UniProtKB - P23930 (LNT_ECOLI)

BLAST

>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
TPYARTGNWPLWVLTALFGFAAVLMSLRQRRK

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History
Entry version 146 (07 Nov 2018)
Sequence version 1 (01 Mar 1992)
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Protein

Apolipoprotein N-acyltransferase

Gene

lnt

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Transfers the fatty acyl group on membrane lipoproteins.

Pathwayⁱ: lipoprotein biosynthesis (N-acyl transfer)

This protein is involved in the pathway lipoprotein biosynthesis (N-acyl transfer), which is part of Protein modification.
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	Length
Active siteⁱ	267	Proton acceptorPROSITE-ProRule annotation	1
Active siteⁱ	335	PROSITE-ProRule annotation	1
Active siteⁱ	387	NucleophilePROSITE-ProRule annotation	1

GO - Molecular functionⁱ

N-acyltransferase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 2032623
- 21676878

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

lipoprotein biosynthetic process
Source: EcoCyc
Inferred from direct assayⁱ
- 2032623
- 21676878

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Transferase
Ligand	Copper

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10168-MONOMER MetaCyc:EG10168-MONOMER
UniPathwayⁱ	UPA00666

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Apolipoprotein N-acyltransferase (EC:2.3.1.-) Short name: ALP N-acyltransferase Alternative name(s): Copper homeostasis protein CutE
Gene namesⁱ	Name:lnt Synonyms:cutE Ordered Locus Names:b0657, JW0654
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10168 cutE

EcoGeneⁱ

EG10168 cutE

Subcellular locationⁱ

Cell inner membrane
2 Publications
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: SUBCELLULAR LOCATION.
- Ref.8
  "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.
; Multi-pass membrane protein
2 Publications
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: SUBCELLULAR LOCATION.
- Ref.8
  "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.

Topology

Feature key	Position(s)	DescriptionActions	Length
Transmembraneⁱ	12 – 28	HelicalSequence analysisAdd BLAST	17
Transmembraneⁱ	57 – 77	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	91 – 111	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	168 – 188	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	194 – 214	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	487 – 507	HelicalSequence analysisAdd BLAST	21

GO - Cellular componentⁱ

integral component of plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 15513925
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000178062	1 – 512	Apolipoprotein N-acyltransferaseAdd BLAST		512

Proteomic databases

PaxDbⁱ	P23930
PRIDEⁱ	P23930

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
pykA	P21599	3	EBI-556569,EBI-368956

With

Entry

#Exp.

IntAct

Notes

pykA

P21599

EBI-556569,EBI-368956

Protein-protein interaction databases

BioGridⁱ	4259916, 206 interactors
Database of interacting proteins More...DIPⁱ	DIP-10111N
IntActⁱ	P23930, 2 interactors
STRINGⁱ	316385.ECDH10B_0726

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	6 – 8	Combined sources	3
Helixⁱ	10 – 23	Combined sources	14
Helixⁱ	24 – 27	Combined sources	4
Turnⁱ	29 – 31	Combined sources	3
Helixⁱ	35 – 47	Combined sources	13
Turnⁱ	48 – 50	Combined sources	3
Helixⁱ	53 – 71	Combined sources	19
Helixⁱ	75 – 83	Combined sources	9
Helixⁱ	87 – 115	Combined sources	29
Helixⁱ	121 – 125	Combined sources	5
Helixⁱ	127 – 139	Combined sources	13
Helixⁱ	142 – 144	Combined sources	3
Helixⁱ	153 – 155	Combined sources	3
Beta strandⁱ	156 – 158	Combined sources	3
Helixⁱ	161 – 163	Combined sources	3
Helixⁱ	164 – 167	Combined sources	4
Helixⁱ	169 – 189	Combined sources	21
Helixⁱ	192 – 203	Combined sources	12
Helixⁱ	206 – 210	Combined sources	5
Beta strandⁱ	214 – 216	Combined sources	3
Helixⁱ	218 – 220	Combined sources	3
Beta strandⁱ	222 – 228	Combined sources	7
Helixⁱ	233 – 236	Combined sources	4
Helixⁱ	239 – 241	Combined sources	3
Helixⁱ	242 – 253	Combined sources	12
Helixⁱ	254 – 256	Combined sources	3
Turnⁱ	257 – 259	Combined sources	3
Beta strandⁱ	261 – 264	Combined sources	4
Beta strandⁱ	270 – 273	Combined sources	4
Helixⁱ	274 – 277	Combined sources	4
Helixⁱ	278 – 290	Combined sources	13
Beta strandⁱ	294 – 304	Combined sources	11
Beta strandⁱ	310 – 320	Combined sources	11
Beta strandⁱ	332 – 334	Combined sources	3
Turnⁱ	341 – 343	Combined sources	3
Helixⁱ	349 – 351	Combined sources	3
Turnⁱ	352 – 356	Combined sources	5
Beta strandⁱ	375 – 377	Combined sources	3
Beta strandⁱ	380 – 386	Combined sources	7
Helixⁱ	387 – 391	Combined sources	5
Helixⁱ	393 – 399	Combined sources	7
Beta strandⁱ	406 – 411	Combined sources	6
Helixⁱ	413 – 416	Combined sources	4
Turnⁱ	417 – 420	Combined sources	4
Helixⁱ	421 – 436	Combined sources	16
Beta strandⁱ	440 – 447	Combined sources	8
Beta strandⁱ	450 – 452	Combined sources	3
Beta strandⁱ	458 – 461	Combined sources	4
Beta strandⁱ	464 – 466	Combined sources	3
Beta strandⁱ	468 – 474	Combined sources	7
Helixⁱ	482 – 486	Combined sources	5
Helixⁱ	489 – 505	Combined sources	17

Show more details

3D structure databases

ProteinModelPortalⁱ	P23930
SMRⁱ	P23930
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	227 – 476	CN hydrolasePROSITE-ProRule annotationAdd BLAST		250

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	425 – 431	Could contain a copper-binding motif		7

Sequence similaritiesⁱ

Belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4105CE8 Bacteria COG0815 LUCA
HOGENOMⁱ	HOG000264279
InParanoidⁱ	P23930
KEGG Orthology (KO) More...KOⁱ	K03820
PhylomeDBⁱ	P23930

Family and domain databases

Conserved Domains Database More...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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

P23930-1 [UniParc]FASTA Add to basket

« Hide

        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

Checksum:ⁱ70CFD6627C286615

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	186	A → V (PubMed:8905232).Curated		1

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
NCBI Reference Sequences More...RefSeqⁱ	NP_415190.1, NC_000913.3 WP_000853021.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73758; AAC73758; b0657 BAA35308; BAA35308; BAA35308
GeneIDⁱ	946201
KEGGⁱ	ecj:JW0654 eco:b0657
PATRICⁱ	fig\|1411691.4.peg.1611

Protein	Similar proteins		Species	Score	Length	Source
P23930	Apolipoprotein N-acyltransferase		Shigella sp.		512	UniRef100_P23930
Apolipoprotein N-acyltransferase		ECOLX		512
Apolipoprotein N-acyltransferase		SHIBO		512
Apolipoprotein N-acyltransferase		Escherichia coli 1-110-08_S3_C1		512
Apolipoprotein N-acyltransferase		Escherichia coli DEC6A		512
+32

Protein	Similar proteins		Species	Score	Length	Source
P23930	Apolipoprotein N-acyltransferase		ECO57		512	UniRef90_P23930
Apolipoprotein N-acyltransferase		ECOL6		512
Apolipoprotein N-acyltransferase		SHIFL		512
Apolipoprotein N-acyltransferase		Shigella sp.		512
Apolipoprotein N-acyltransferase		ECOLX		512
+788

Protein	Similar proteins		Species	Score	Length	Source
P23930	Apolipoprotein N-acyltransferase		ECOL6		512	UniRef50_P23930
Apolipoprotein N-acyltransferase		SHIFL		512
Apolipoprotein N-acyltransferase		ECO57		512
Apolipoprotein N-acyltransferase		YERPE		515
Apolipoprotein N-acyltransferase		SALTY		512
+2767

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_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links 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	[»]
	5VRG	X-ray	2.52	A	2-512	[»]
	5VRH	X-ray	2.14	A	2-512	[»]
	5XHQ	X-ray	2.59	A/B	1-508	[»]
ProteinModelPortalⁱ	P23930
SMRⁱ	P23930
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4259916, 206 interactors
DIPⁱ	DIP-10111N
IntActⁱ	P23930, 2 interactors
STRINGⁱ	316385.ECDH10B_0726

Proteomic databases

PaxDbⁱ	P23930
PRIDEⁱ	P23930

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

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

EchoBASEⁱ	EB0166
EcoGeneⁱ	EG10168 cutE

Phylogenomic databases

eggNOGⁱ	ENOG4105CE8 Bacteria COG0815 LUCA
HOGENOMⁱ	HOG000264279
InParanoidⁱ	P23930
KOⁱ	K03820
PhylomeDBⁱ	P23930

Enzyme and pathway databases

UniPathwayⁱ	UPA00666
BioCycⁱ	EcoCyc:EG10168-MONOMER MetaCyc:EG10168-MONOMER

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P23930

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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LNT_ECOLI
Accessionⁱ	P23930Primary (citable) accession number: P23930 Secondary accession number(s): P77703
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
	Last sequence update:	March 1, 1992
	Last modified:	November 7, 2018
	This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P23930 (LNT_ECOLI)

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Apolipoprotein N-acyltransferase

lnt

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'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)

Sites

<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

GO - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<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

Proteomic databases

<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

Protein-protein interaction databases

<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

3D structure databases

<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

Region

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

Pathwayⁱ: lipoprotein biosynthesis (N-acyl transfer)

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ