UniProtKB - P23930 (LNT_ECOLI)
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>sp|P23930|LNT_ECOLI Apolipoprotein N-acyltransferase OS=Escherichia coli (strain K12) OX=83333 GN=lnt PE=1 SV=1 MAFASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLMGLQALTFNRRPLQSAAIG FCWGFGLFGSGINWVYVSIATFGGMPGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTT WLRVAIAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKGLAPIMGVEAINFLLMMVS GLLALALVKRNWRPLVVAVVLFALPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEG QLLNTLKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRDKGSSLVTGIV DARLNKQNRYDTYNTIITLGKGAPYSYESADRYNKNHLVPFGEFVPLESILRPLAPFFDL PMSSFSRGPYIQPPLSANGIELTAAICYEIILGEQVRDNFRPDTDYLLTISNDAWFGKSI GPWQHFQMARMRALELARPLLRSTNNGITAVIGPQGEIQAMIPQFTREVLTTNVTPTTGL TPYARTGNWPLWVLTALFGFAAVLMSLRQRRKCommunity curation ()Add a publicationFeedback
Protein
Apolipoprotein N-acyltransferase
Gene
lnt
Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation (PubMed:2032623, PubMed:21676878, PubMed:28885614, PubMed:28675161). Utilizes a two-step reaction via a ping-pong mechanism (PubMed:21676878, PubMed:28675161). Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein (PubMed:21676878, PubMed:28675161). In vitro, can utilize the phospholipids phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidic acid (PA) or cardiolipin (CL) (PubMed:2032623, PubMed:21676878). PE is the most efficient acyl donor (PubMed:21676878).1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.7"Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase."
Gupta S.D., Gan K., Schmid M.B., Wu H.C.
J. Biol. Chem. 268:16551-16556(1993) [PubMed] [Europe PMC] [Abstract]Cited for: PROBABLE FUNCTION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli."
Gupta S.D., Wu H.C.
FEMS Microbiol. Lett. 62:37-41(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.11"Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase."
Hillmann F., Argentini M., Buddelmeijer N.
J. Biol. Chem. 286:27936-27946(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM. - Ref.12"Crystal structure of E. coli apolipoprotein N-acyl transferase."
Lu G., Xu Y., Zhang K., Xiong Y., Li H., Cui L., Wang X., Lou J., Zhai Y., Sun F., Zhang X.C.
Nat. Commun. 8:15948-15948(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-508, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF SER-78; GLY-145; GLU-267; LYS-335; VAL-339; GLY-342; GLU-343; ARG-352; CYS-387; TYR-388; GLU-389 AND PHE-416. - Ref.13"Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis."
Wiktor M., Weichert D., Howe N., Huang C.Y., Olieric V., Boland C., Bailey J., Vogeley L., Stansfeld P.J., Buddelmeijer N., Wang M., Caffrey M.
Nat. Commun. 8:15952-15952(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-387, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBCELLULAR LOCATION, TOPOLOGY, ACTIVE SITE, MUTAGENESIS OF GLU-267; LYS-335 AND CYS-387.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- a glycerophospholipidEC:2.3.1.269
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- See the description of this molecule in ChEBI.
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<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.11"Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase."
Hillmann F., Argentini M., Buddelmeijer N.
J. Biol. Chem. 286:27936-27946(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM. - Ref.12"Crystal structure of E. coli apolipoprotein N-acyl transferase."
Lu G., Xu Y., Zhang K., Xiong Y., Li H., Cui L., Wang X., Lou J., Zhai Y., Sun F., Zhang X.C.
Nat. Commun. 8:15948-15948(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-508, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF SER-78; GLY-145; GLU-267; LYS-335; VAL-339; GLY-342; GLU-343; ARG-352; CYS-387; TYR-388; GLU-389 AND PHE-416. - Ref.13"Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis."
Wiktor M., Weichert D., Howe N., Huang C.Y., Olieric V., Boland C., Bailey J., Vogeley L., Stansfeld P.J., Buddelmeijer N., Wang M., Caffrey M.
Nat. Commun. 8:15952-15952(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-387, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBCELLULAR LOCATION, TOPOLOGY, ACTIVE SITE, MUTAGENESIS OF GLU-267; LYS-335 AND CYS-387.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.11"Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase."
Hillmann F., Argentini M., Buddelmeijer N.
J. Biol. Chem. 286:27936-27946(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM. - Ref.12"Crystal structure of E. coli apolipoprotein N-acyl transferase."
Lu G., Xu Y., Zhang K., Xiong Y., Li H., Cui L., Wang X., Lou J., Zhai Y., Sun F., Zhang X.C.
Nat. Commun. 8:15948-15948(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-508, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF SER-78; GLY-145; GLU-267; LYS-335; VAL-339; GLY-342; GLU-343; ARG-352; CYS-387; TYR-388; GLU-389 AND PHE-416. - Ref.13"Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis."
Wiktor M., Weichert D., Howe N., Huang C.Y., Olieric V., Boland C., Bailey J., Vogeley L., Stansfeld P.J., Buddelmeijer N., Wang M., Caffrey M.
Nat. Commun. 8:15952-15952(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-387, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBCELLULAR LOCATION, TOPOLOGY, ACTIVE SITE, MUTAGENESIS OF GLU-267; LYS-335 AND CYS-387.
Source: Rhea- Search for this reaction in UniProtKB.
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a glycerophospholipid- Search proteins in UniProtKB for this molecule.
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+N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]- Search proteins in UniProtKB for this molecule.
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N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinezoom- Search proteins in UniProtKB for this molecule.
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=a 1-lyso-glycerophospholipid- Search proteins in UniProtKB for this molecule.
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+N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]- Search proteins in UniProtKB for this molecule.
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N-acyl-(S-1,2-diacyl-sn-glyceryl)-L-cysteine residuezoom- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: lipoprotein biosynthesis (N-acyl transfer)
This protein is involved in the pathway lipoprotein biosynthesis (N-acyl transfer), which is part of Protein modification.UniRule annotationManual assertion according to rulesi
View all proteins of this organism that are known to be involved in the pathway lipoprotein biosynthesis (N-acyl transfer) and in Protein modification.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 267 | Proton acceptorUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 1 | |
| Active sitei | 335 | UniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 1 | |
| Active sitei | 387 | NucleophileUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- N-acyltransferase activity Source: EcoCyc
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.6"Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli."
Gupta S.D., Wu H.C.
FEMS Microbiol. Lett. 62:37-41(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.11"Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase."
Hillmann F., Argentini M., Buddelmeijer N.
J. Biol. Chem. 286:27936-27946(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM.
GO - Biological processi
- lipoprotein biosynthetic process Source: EcoCycInferred from direct assayi
- Ref.6"Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli."
Gupta S.D., Wu H.C.
FEMS Microbiol. Lett. 62:37-41(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.11"Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase."
Hillmann F., Argentini M., Buddelmeijer N.
J. Biol. Chem. 286:27936-27946(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Acyltransferase, Transferase |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10168-MONOMER MetaCyc:EG10168-MONOMER |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00666 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Apolipoprotein N-acyltransferase1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion according to rulesi (EC:2.3.1.269
Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
Short name: ALP N-acyltransferase1 Publication Manual assertion based on opinion ini
Manual assertion according to rulesi Alternative name(s): Copper homeostasis protein CutE |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:lnt1 Publication Manual assertion based on opinion ini
Manual assertion according to rulesi Synonyms:cutE1 Publication Manual assertion based on opinion ini
Ordered Locus Names:b0657, JW0654 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Escherichia coli (strain K12) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83333 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
- Cell inner membrane UniRule annotation
Manual assertion according to rulesi
5 PublicationsManual assertion based on experiment ini
- Ref.6"Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli."
Gupta S.D., Wu H.C.
FEMS Microbiol. Lett. 62:37-41(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.8"Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli."
Robichon C., Vidal-Ingigliardi D., Pugsley A.P.
J. Biol. Chem. 280:974-983(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. - Ref.9"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.12"Crystal structure of E. coli apolipoprotein N-acyl transferase."
Lu G., Xu Y., Zhang K., Xiong Y., Li H., Cui L., Wang X., Lou J., Zhai Y., Sun F., Zhang X.C.
Nat. Commun. 8:15948-15948(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-508, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF SER-78; GLY-145; GLU-267; LYS-335; VAL-339; GLY-342; GLU-343; ARG-352; CYS-387; TYR-388; GLU-389 AND PHE-416. - Ref.13"Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis."
Wiktor M., Weichert D., Howe N., Huang C.Y., Olieric V., Boland C., Bailey J., Vogeley L., Stansfeld P.J., Buddelmeijer N., Wang M., Caffrey M.
Nat. Commun. 8:15952-15952(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-387, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBCELLULAR LOCATION, TOPOLOGY, ACTIVE SITE, MUTAGENESIS OF GLU-267; LYS-335 AND CYS-387.
Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.8"Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli."
Robichon C., Vidal-Ingigliardi D., Pugsley A.P.
J. Biol. Chem. 280:974-983(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. - Ref.12"Crystal structure of E. coli apolipoprotein N-acyl transferase."
Lu G., Xu Y., Zhang K., Xiong Y., Li H., Cui L., Wang X., Lou J., Zhai Y., Sun F., Zhang X.C.
Nat. Commun. 8:15948-15948(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-508, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF SER-78; GLY-145; GLU-267; LYS-335; VAL-339; GLY-342; GLU-343; ARG-352; CYS-387; TYR-388; GLU-389 AND PHE-416. - Ref.13"Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis."
Wiktor M., Weichert D., Howe N., Huang C.Y., Olieric V., Boland C., Bailey J., Vogeley L., Stansfeld P.J., Buddelmeijer N., Wang M., Caffrey M.
Nat. Commun. 8:15952-15952(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-387, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBCELLULAR LOCATION, TOPOLOGY, ACTIVE SITE, MUTAGENESIS OF GLU-267; LYS-335 AND CYS-387.
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 9 | Cytoplasmic2 Publications Manual assertion based on experiment ini
| 9 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 10 – 27 | Helical1 Publication Manual assertion based on experiment ini
| 18 | |
| Topological domaini | 28 – 33 | Periplasmic2 Publications Manual assertion based on experiment ini
| 6 | |
| Transmembranei | 34 – 48 | Helical1 Publication Manual assertion based on experiment ini
| 15 | |
| Topological domaini | 49 – 52 | Cytoplasmic2 Publications Manual assertion based on experiment ini
| 4 | |
| Transmembranei | 53 – 68 | Helical1 Publication Manual assertion based on experiment ini
| 16 | |
| Topological domaini | 69 – 86 | Periplasmic2 Publications Manual assertion based on experiment ini
| 18 | |
| Transmembranei | 87 – 116 | Helical1 Publication Manual assertion based on experiment ini
| 30 | |
| Topological domaini | 117 – 120 | Cytoplasmic2 Publications Manual assertion based on experiment ini
| 4 | |
| Transmembranei | 121 – 141 | Helical1 Publication Manual assertion based on experiment ini
| 21 | |
| Topological domaini | 142 – 168 | Periplasmic2 Publications Manual assertion based on experiment ini
| 27 | |
| Transmembranei | 169 – 189 | Helical1 Publication Manual assertion based on experiment ini
| 21 | |
| Topological domaini | 190 – 191 | Cytoplasmic2 Publications Manual assertion based on experiment ini
| 2 | |
| Transmembranei | 192 – 210 | Helical1 Publication Manual assertion based on experiment ini
| 19 | |
| Topological domaini | 211 – 487 | Periplasmic2 Publications Manual assertion based on experiment ini
| 277 | |
| Transmembranei | 488 – 508 | Helical1 Publication Manual assertion based on experiment ini
| 21 | |
| Topological domaini | 509 – 512 | Cytoplasmic2 Publications Manual assertion based on experiment ini
| 4 |
GO - Cellular componenti
- integral component of plasma membrane Source: EcoCycInferred from direct assayi
- Ref.8"Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli."
Robichon C., Vidal-Ingigliardi D., Pugsley A.P.
J. Biol. Chem. 280:974-983(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
- outer membrane-bounded periplasmic space Source: EcoCycInferred from direct assayi
- Ref.8"Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli."
Robichon C., Vidal-Ingigliardi D., Pugsley A.P.
J. Biol. Chem. 280:974-983(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
- plasma membrane Source: EcoCycInferred from direct assayi
- Ref.9"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS."
Zhang N., Chen R., Young N., Wishart D., Winter P., Weiner J.H., Li L.
Proteomics 7:484-493(2007) [PubMed] [Europe PMC] [Abstract] - Ref.6"Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli."
Gupta S.D., Wu H.C.
FEMS Microbiol. Lett. 62:37-41(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
Essential. Depletion induces juxtapositioning of inner and outer membranes and alters the architecture of the cell envelope. It causes mislocalization of outer membrane lipoproteins (PubMed:15513925). The mutant has a copper-sensitive, temperature sensitive phenotype (PubMed:1938881).2 Publications
Manual assertion based on experiment ini
- Ref.1"Cloning and characterization of cutE, a gene involved in copper transport in Escherichia coli."
Rogers S.D., Bhave M.R., Mercer J.F.B., Camakaris J., Lee B.T.O.
J. Bacteriol. 173:6742-6748(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE. - Ref.8"Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli."
Robichon C., Vidal-Ingigliardi D., Pugsley A.P.
J. Biol. Chem. 280:974-983(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 78 | S → W: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 145 | G → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 148 | W → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 237 | W → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 267 | E → A or Q: Loss of activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 335 | K → A: Loss of activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 339 | V → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 339 | V → G: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 342 | G → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 343 | E → A: Loss of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 352 | R → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 387 | C → A or S: Loss of activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 388 | Y → A or W: Loss of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 389 | E → A: Loss of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 416 | F → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000178062 | 1 – 512 | Apolipoprotein N-acyltransferaseAdd BLAST | 512 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P23930 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P23930 |
PRoteomics IDEntifications database More...PRIDEi | P23930 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Monomer.
1 PublicationManual assertion based on experiment ini
- Ref.12"Crystal structure of E. coli apolipoprotein N-acyl transferase."
Lu G., Xu Y., Zhang K., Xiong Y., Li H., Cui L., Wang X., Lou J., Zhai Y., Sun F., Zhang X.C.
Nat. Commun. 8:15948-15948(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-508, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF SER-78; GLY-145; GLU-267; LYS-335; VAL-339; GLY-342; GLU-343; ARG-352; CYS-387; TYR-388; GLU-389 AND PHE-416.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
P23930
| With | #Exp. | IntAct |
|---|---|---|
| pykA [P21599] | 3 | EBI-556569,EBI-368956 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4259916, 206 interactors 850561, 1 interactor |
Database of interacting proteins More...DIPi | DIP-10111N |
Protein interaction database and analysis system More...IntActi | P23930, 2 interactors |
STRING: functional protein association networks More...STRINGi | 511145.b0657 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 11 – 25 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 29 – 31 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 35 – 47 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Turni | 48 – 50 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 53 – 71 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| Helixi | 75 – 82 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 88 – 115 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 28 | |
| Helixi | 121 – 125 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 127 – 139 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 142 – 144 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 151 – 157 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 161 – 163 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 164 – 167 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 169 – 188 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| Helixi | 192 – 203 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 206 – 210 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 214 – 216 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 218 – 220 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 222 – 228 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Turni | 233 – 237 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 239 – 241 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 242 – 253 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 254 – 256 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 257 – 259 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 261 – 273 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 274 – 277 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 278 – 291 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| Beta strandi | 294 – 303 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 311 – 320 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 332 – 334 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 340 – 343 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 349 – 351 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 352 – 356 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 375 – 377 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 380 – 386 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 387 – 391 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 393 – 399 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 406 – 411 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 414 – 416 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 421 – 436 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| Beta strandi | 440 – 447 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 449 – 452 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 458 – 462 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 464 – 466 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 468 – 474 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 482 – 486 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 489 – 502 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P23930 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 227 – 476 | CN hydrolaseUniRule annotation Manual assertion according to rulesi Add BLAST | 250 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily.UniRule annotation
Manual assertion according to rulesi
CuratedKeywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG0815, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_019563_3_0_6 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P23930 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P23930 |
Family and domain databases
Conserved Domains Database More...CDDi | cd07571, ALP_N-acyl_transferase, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.60.110.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_01148, Lnt, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR004563, Apolipo_AcylTrfase IPR003010, C-N_Hydrolase IPR036526, C-N_Hydrolase_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00795, CN_hydrolase, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56317, SSF56317, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00546, lnt, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50263, CN_HYDROLASE, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
P23930-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MAFASLIERQ RIRLLLALLF GACGTLAFSP YDVWPAAIIS LMGLQALTFN
60 70 80 90 100
RRPLQSAAIG FCWGFGLFGS GINWVYVSIA TFGGMPGPVN IFLVVLLAAY
110 120 130 140 150
LSLYTGLFAG VLSRLWPKTT WLRVAIAAPA LWQVTEFLRG WVLTGFPWLQ
160 170 180 190 200
FGYSQIDGPL KGLAPIMGVE AINFLLMMVS GLLALALVKR NWRPLVVAVV
210 220 230 240 250
LFALPFPLRY IQWFTPQPEK TIQVSMVQGD IPQSLKWDEG QLLNTLKIYY
260 270 280 290 300
NATAPLMGKS SLIIWPESAI TDLEINQQPF LKALDGELRD KGSSLVTGIV
310 320 330 340 350
DARLNKQNRY DTYNTIITLG KGAPYSYESA DRYNKNHLVP FGEFVPLESI
360 370 380 390 400
LRPLAPFFDL PMSSFSRGPY IQPPLSANGI ELTAAICYEI ILGEQVRDNF
410 420 430 440 450
RPDTDYLLTI SNDAWFGKSI GPWQHFQMAR MRALELARPL LRSTNNGITA
460 470 480 490 500
VIGPQGEIQA MIPQFTREVL TTNVTPTTGL TPYARTGNWP LWVLTALFGF
510
AAVLMSLRQR RK
Length:512
Mass (Da):57,066
Last modified:March 1, 1992 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i70CFD6627C286615
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 186 | A → V (PubMed:8905232).Curated | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X58070 Genomic DNA Translation: CAA41100.1 U82598 Genomic DNA Translation: AAB40859.1 U00096 Genomic DNA Translation: AAC73758.1 AP009048 Genomic DNA Translation: BAA35308.2 |
Protein sequence database of the Protein Information Resource More...PIRi | S18194 |
NCBI Reference Sequences More...RefSeqi | NP_415190.1, NC_000913.3 WP_000853021.1, NZ_SSZK01000037.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC73758; AAC73758; b0657 BAA35308; BAA35308; BAA35308 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 946201 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW0654 eco:b0657 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.1611 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P23930 | Apolipoprotein N-acyltransferase | 512 | UniRef100_P23930 | |||
| Apolipoprotein N-acyltransferase | 512 | |||||
| Apolipoprotein N-acyltransferase | 512 | |||||
| Apolipoprotein N-acyltransferase | 512 | |||||
| Apolipoprotein N-acyltransferase | 512 | |||||
| +40 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P23930 | Apolipoprotein N-acyltransferase | 512 | UniRef90_P23930 | |||
| Apolipoprotein N-acyltransferase | 512 | |||||
| Apolipoprotein N-acyltransferase | ) | 512 | ||||
| Apolipoprotein N-acyltransferase | 512 | |||||
| Apolipoprotein N-acyltransferase | 512 | |||||
| +1061 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P23930 | Apolipoprotein N-acyltransferase | ) | 512 | UniRef50_P23930 | ||
| Apolipoprotein N-acyltransferase | 512 | |||||
| Apolipoprotein N-acyltransferase | 512 | |||||
| Apolipoprotein N-acyltransferase | 512 | |||||
| Apolipoprotein N-acyltransferase | 512 | |||||
| +4427 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X58070 Genomic DNA Translation: CAA41100.1 U82598 Genomic DNA Translation: AAB40859.1 U00096 Genomic DNA Translation: AAC73758.1 AP009048 Genomic DNA Translation: BAA35308.2 |
| PIRi | S18194 |
| RefSeqi | NP_415190.1, NC_000913.3 WP_000853021.1, NZ_SSZK01000037.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 5N6H | X-ray | 2.90 | A/B | 1-512 | [»] | |
| 5N6L | X-ray | 2.90 | A/B | 1-512 | [»] | |
| 5XHQ | X-ray | 2.59 | A/B | 1-508 | [»] | |
| 6NWR | X-ray | 3.50 | A/B | 1-512 | [»] | |
| 6Q3A | X-ray | 3.10 | A | 1-512 | [»] | |
| SMRi | P23930 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 4259916, 206 interactors 850561, 1 interactor |
| DIPi | DIP-10111N |
| IntActi | P23930, 2 interactors |
| STRINGi | 511145.b0657 |
Proteomic databases
| jPOSTi | P23930 |
| PaxDbi | P23930 |
| PRIDEi | P23930 |
Genome annotation databases
| EnsemblBacteriai | AAC73758; AAC73758; b0657 BAA35308; BAA35308; BAA35308 |
| GeneIDi | 946201 |
| KEGGi | ecj:JW0654 eco:b0657 |
| PATRICi | fig|1411691.4.peg.1611 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0166 |
Phylogenomic databases
| eggNOGi | COG0815, Bacteria |
| HOGENOMi | CLU_019563_3_0_6 |
| InParanoidi | P23930 |
| PhylomeDBi | P23930 |
Enzyme and pathway databases
| UniPathwayi | UPA00666 |
| BioCyci | EcoCyc:EG10168-MONOMER MetaCyc:EG10168-MONOMER |
Miscellaneous databases
Protein Ontology More...PROi | PR:P23930 |
Family and domain databases
| CDDi | cd07571, ALP_N-acyl_transferase, 1 hit |
| Gene3Di | 3.60.110.10, 1 hit |
| HAMAPi | MF_01148, Lnt, 1 hit |
| InterProi | View protein in InterPro IPR004563, Apolipo_AcylTrfase IPR003010, C-N_Hydrolase IPR036526, C-N_Hydrolase_sf |
| Pfami | View protein in Pfam PF00795, CN_hydrolase, 1 hit |
| SUPFAMi | SSF56317, SSF56317, 1 hit |
| TIGRFAMsi | TIGR00546, lnt, 1 hit |
| PROSITEi | View protein in PROSITE PS50263, CN_HYDROLASE, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | LNT_ECOLI | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P23930Primary (citable) accession number: P23930 Secondary accession number(s): P77703 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 1, 1992 |
| Last sequence update: | March 1, 1992 | |
| Last modified: | December 2, 2020 | |
| This is version 160 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
