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UniProtKB - P0A924 (PGPB_ECOLI)

Entry version 107 (18 Sep 2019)
Sequence version 1 (19 Jul 2005)
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Protein

Phosphatidylglycerophosphatase B

Gene

pgpB

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>

<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 dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. The pattern of activities varies according to subcellular location, PGP phosphatase activity is higher in the cytoplasmic membrane, whereas PA and LPA phosphatase activities are higher in the outer membrane. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide.4 Publications

Miscellaneous

The enzyme active site contains a catalytic triad that establishes a charge relay system. This catalytic triad is essential for the dephosphorylation of LPA, PA, and sphingosine-1-phosphate, but is not essential in its entirety for the dephosphorylation of PGP, the nucleophilic histidine alone is sufficient to hydrolyze PGP.1 Publication

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by Mn2+ ions. Inhibited by phosphatidylethanolamine (PE) (PubMed:27405756).1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=530 µM for undecaprenyl pyrophosphate2 Publications
  2. KM=96 µM for farnesyl pyrophosphate2 Publications
  3. KM=80 µM for diacylglycerol pyrophosphate2 Publications
  4. KM=1700 µM for phosphatidate2 Publications
  1. Vmax=2167 nmol/min/mg enzyme with diacylglycerol pyrophosphate as substrate2 Publications
  2. Vmax=313 nmol/min/mg enzyme with phosphatidate as substrate2 Publications

pH dependencei

Optimum pH is 6.5 for DGPP phosphatase activity and 6.5-7.5 for undecaprenyl pyrophosphate phosphatase activity.2 Publications

<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: phosphatidylglycerol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes phosphatidylglycerol from CDP-diacylglycerol.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (pgsA), CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (pgsA)
  2. Phosphatidylglycerophosphatase A (pgpA), Phosphatidylglycerophosphatase B (pgpB), Phosphatidylglycerophosphatase A (pgpA), Phosphatidylglycerophosphatase A (pgpA), Phosphatidylglycerophosphatase C (pgpC)
This subpathway is part of the pathway phosphatidylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylglycerol from CDP-diacylglycerol, the pathway phosphatidylglycerol biosynthesis and in Phospholipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei163Proton donor; for a subset of substrates1 Publication1
Active sitei207Nucleophile1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei211Stabilizes the active site histidine for nucleophilic attack1 Publication1

<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

  • diacylglycerol diphosphate phosphatase activity Source: UniProtKB-EC
  • phosphatidate phosphatase activity Source: UniProtKB-EC
  • phosphatidylglycerophosphatase activity Source: EcoCyc
  • undecaprenyl-diphosphatase activity Source: EcoCyc
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHydrolase
Biological processLipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:PGPPHOSPHAB-MONOMER
ECOL316407:JW1270-MONOMER
MetaCyc:PGPPHOSPHAB-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00084;UER00504

<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_and_taxonomy_section">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:
Phosphatidylglycerophosphatase B (EC:3.1.3.27)
Alternative name(s):
Diacylglycerol pyrophosphate phosphatase (EC:3.1.3.81)
Short name:
DGPP phosphatase
Phosphatidate phosphatase (EC:3.1.3.4)
Undecaprenyl pyrophosphate phosphatase (EC:3.6.1.27)
Undecaprenyl-diphosphatase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:pgpB
Ordered Locus Names:b1278, JW1270
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10705 pgpB

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei2 – 24Helical1 PublicationAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 domaini25 – 54Periplasmic1 PublicationAdd BLAST30
Transmembranei55 – 66Helical1 PublicationAdd BLAST12
Topological domaini67 – 71Cytoplasmic1 Publication5
Transmembranei72 – 94Helical1 PublicationAdd BLAST23
Topological domaini95 – 161Periplasmic1 PublicationAdd BLAST67
Transmembranei162 – 176Helical1 PublicationAdd BLAST15
Topological domaini177 – 182Cytoplasmic1 Publication6
Transmembranei183 – 202Helical1 PublicationAdd BLAST20
Topological domaini203 – 208Periplasmic1 Publication6
Transmembranei209 – 232Helical1 PublicationAdd BLAST24
Topological domaini233 – 254Cytoplasmic1 PublicationAdd BLAST22

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cell outer membrane, Membrane

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000583622 – 254Phosphatidylglycerophosphatase BAdd BLAST253

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P0A924

PRoteomics IDEntifications database

More...PRIDEi		P0A924

<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

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4262195, 215 interactors

Protein interaction database and analysis system

More...IntActi		P0A924, 1 interactor

STRING: functional protein association networks

More...STRINGi		511145.b1278

<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

1254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P0A924

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni97 – 105Phosphatase sequence motif ICurated9
Regioni160 – 163Phosphatase sequence motif IICurated4
Regioni200 – 211Phosphatase sequence motif IIICuratedAdd BLAST12

<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 PA-phosphatase related phosphoesterase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105EYK Bacteria
COG0671 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000286191

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A924

KEGG Orthology (KO)

More...KOi		K01096

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036938 P_Acid_Pase_2/haloperoxi_sf
IPR000326 P_Acid_Pase_2/haloperoxidase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01569 PAP2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00014 acidPPc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48317 SSF48317, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A924-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRSIARRTAV GAALLLVMPV AVWISGWRWQ PGEQSWLLKA AFWVTETVTQ 
        60         70         80         90        100
PWGVITHLIL FGWFLWCLRF RIKAAFVLFA ILAAAILVGQ GVKSWIKDKV 
       110        120        130        140        150
QEPRPFVIWL EKTHHIPVDE FYTLKRAERG NLVKEQLAEE KNIPQYLRSH 
       160        170        180        190        200
WQKETGFAFP SGHTMFAASW ALLAVGLLWP RRRTLTIAIL LVWATGVMGS 
       210        220        230        240        250
RLLLGMHWPR DLVVATLISW ALVAVATWLA QRICGPLTPP AEENREIAQR 

EQES
Length:254
Mass (Da):29,021
Last modified:July 19, 2005 - 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:i9F4E6E88C34D458C
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 30151 Da from positions 2 - 254. Determined by MALDI. Reported mass includes mass of a C-terminal His6 tag.1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M23628 Unassigned DNA Translation: AAB36618.1
U00096 Genomic DNA Translation: AAC74360.1
AP009048 Genomic DNA Translation: BAA14832.1

Protein sequence database of the Protein Information Resource

More...PIRi		A30193 PAECGB

NCBI Reference Sequences

More...RefSeqi		NP_415794.1, NC_000913.3
WP_001256538.1, NZ_STEB01000005.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74360; AAC74360; b1278
BAA14832; BAA14832; BAA14832

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945863

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1270
eco:b1278

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1003

<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

<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
M23628 Unassigned DNA Translation: AAB36618.1
U00096 Genomic DNA Translation: AAC74360.1
AP009048 Genomic DNA Translation: BAA14832.1
PIRiA30193 PAECGB
RefSeqiNP_415794.1, NC_000913.3
WP_001256538.1, NZ_STEB01000005.1

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 entryMethodResolution (Å)ChainPositionsPDBsum
4PX7X-ray3.20A2-254[»]
5JWYX-ray3.20A1-254[»]
SMRiP0A924
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4262195, 215 interactors
IntActiP0A924, 1 interactor
STRINGi511145.b1278

Proteomic databases

PaxDbiP0A924
PRIDEiP0A924

Genome annotation databases

EnsemblBacteriaiAAC74360; AAC74360; b1278
BAA14832; BAA14832; BAA14832
GeneIDi945863
KEGGiecj:JW1270
eco:b1278
PATRICifig|1411691.4.peg.1003

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0699
EcoGeneiEG10705 pgpB

Phylogenomic databases

eggNOGiENOG4105EYK Bacteria
COG0671 LUCA
HOGENOMiHOG000286191
InParanoidiP0A924
KOiK01096

Enzyme and pathway databases

UniPathwayiUPA00084;UER00504
BioCyciEcoCyc:PGPPHOSPHAB-MONOMER
ECOL316407:JW1270-MONOMER
MetaCyc:PGPPHOSPHAB-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:P0A924

Family and domain databases

InterProiView protein in InterPro
IPR036938 P_Acid_Pase_2/haloperoxi_sf
IPR000326 P_Acid_Pase_2/haloperoxidase
PfamiView protein in Pfam
PF01569 PAP2, 1 hit
SMARTiView protein in SMART
SM00014 acidPPc, 1 hit
SUPFAMiSSF48317 SSF48317, 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 nameiPGPB_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>AccessioniPrimary (citable) accession number: P0A924
Secondary accession number(s): P18201
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: September 18, 2019
This is version 107 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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