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Entry version 120 (13 Nov 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Phosphate acetyltransferase

Gene

pta

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

Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP.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 NADH and ATP. Pyruvate and PEP act as activators of the acetyl phosphate forming reaction while inhibiting the formation of acetyl-CoA.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=67.2 µM for acetyl-CoA1 Publication
  2. KM=44.9 µM for acetyl phosphate1 Publication
  1. Vmax=177.4 µM/h/mg enzyme for acetyl-CoA-forming reaction1 Publication
  2. Vmax=23.1 µM/h/mg enzyme for acetyl phosphate-forming reaction1 Publication

<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: acetyl-CoA biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes acetyl-CoA from acetate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Acetate kinase (ackA), Acetate kinase (ackA), Acetate kinase (tdcD)
  2. Phosphate acetyltransferase (FAM12_06650), Phosphate acetyltransferase (pta), Phosphate acetyltransferase (FAM11_09405)
This subpathway is part of the pathway acetyl-CoA biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from acetate, the pathway acetyl-CoA biosynthesis and in Metabolic intermediate biosynthesis.

<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

<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 functionAcyltransferase, Transferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:PHOSACETYLTRANS-MONOMER
ECOL316407:JW2294-MONOMER
MetaCyc:PHOSACETYLTRANS-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.1.8 2026

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

More...
UniPathwayi
UPA00340;UER00459

<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:
Phosphate acetyltransferase (EC:2.3.1.8)
Alternative name(s):
Phosphotransacetylase
<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:pta
Ordered Locus Names:b2297, JW2294
<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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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

<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

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<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

Severe impairment of growth in anaerobic conditions, as well as in growth on minimal medium. Increased sensitivity to environmental changes. Poor starvation survival and slower growth on glucose, fructose, tryptone broth, or pyruvate, but normal growth on glycerol or succinate.2 Publications

<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 methionineiRemoved2 Publications
<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_00001791292 – 714Phosphate acetyltransferaseAdd BLAST713

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A9M8

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9M8

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

More...
PaxDbi
P0A9M8

PRoteomics IDEntifications database

More...
PRIDEi
P0A9M8

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0A9M8

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261500, 351 interactors
851119, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-35815N

Protein interaction database and analysis system

More...
IntActi
P0A9M8, 28 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2297

<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

3D structure databases

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

More...
SMRi
P0A9M8

Database of comparative protein structure models

More...
ModBasei
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>Regioni391 – 714Phosphate acetyltransferaseAdd BLAST324

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site.1 Publication

<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

In the N-terminal section; belongs to the CobB/CobQ family.Curated
In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C6K Bacteria
COG0280 LUCA
COG0857 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000053797

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9M8

KEGG Orthology (KO)

More...
KOi
K13788

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9M8

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1390.20, 1 hit
3.40.50.10750, 1 hit
3.40.50.10950, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010766 DRTGG
IPR016475 P-Actrans_bac
IPR027417 P-loop_NTPase
IPR004614 P_AcTrfase
IPR042113 P_AcTrfase_dom1
IPR042112 P_AcTrfase_dom2
IPR002505 PTA_PTB
IPR028979 Ser_kin/Pase_Hpr-like_N_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07085 DRTGG, 1 hit
PF01515 PTA_PTB, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF006107 PhpActrans_proteobac, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit
SSF75138 SSF75138, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00651 pta, 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.

P0A9M8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRTGGDAP
60 70 80 90 100
DQTTTIVRAN SSTTTAAEPL KMSYVEGLLS SNQKDVLMEE IVANYHANTK
110 120 130 140 150
DAEVVLVEGL VPTRKHQFAQ SLNYEIAKTL NAEIVFVMSQ GTDTPEQLKE
160 170 180 190 200
RIELTRNSFG GAKNTNITGV IVNKLNAPVD EQGRTRPDLS EIFDDSSKAK
210 220 230 240 250
VNNVDPAKLQ ESSPLPVLGA VPWSFDLIAT RAIDMARHLN ATIINEGDIN
260 270 280 290 300
TRRVKSVTFC ARSIPHMLEH FRAGSLLVTS ADRPDVLVAA CLAAMNGVEI
310 320 330 340 350
GALLLTGGYE MDARISKLCE RAFATGLPVF MVNTNTWQTS LSLQSFNLEV
360 370 380 390 400
PVDDHERIEK VQEYVANYIN ADWIESLTAT SERSRRLSPP AFRYQLTELA
410 420 430 440 450
RKAGKRIVLP EGDEPRTVKA AAICAERGIA TCVLLGNPAE INRVAASQGV
460 470 480 490 500
ELGAGIEIVD PEVVRESYVG RLVELRKNKG MTETVAREQL EDNVVLGTLM
510 520 530 540 550
LEQDEVDGLV SGAVHTTANT IRPPLQLIKT APGSSLVSSV FFMLLPEQVY
560 570 580 590 600
VYGDCAINPD PTAEQLAEIA IQSADSAAAF GIEPRVAMLS YSTGTSGAGS
610 620 630 640 650
DVEKVREATR LAQEKRPDLM IDGPLQYDAA VMADVAKSKA PNSPVAGRAT
660 670 680 690 700
VFIFPDLNTG NTTYKAVQRS ADLISIGPML QGMRKPVNDL SRGALVDDIV
710
YTIALTAIQS AQQQ
Length:714
Mass (Da):77,172
Last modified:January 23, 2007 - v2
<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:iB45AF0C93494A04C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti20 – 50SLGVI…GGDAP → AWRDPCNGTQRRSSERFQTY RSAAYRWRCA in BAA04663 (PubMed:7918659).CuratedAdd BLAST31
Sequence conflicti208 – 209KL → NV in BAA04502 (PubMed:7883769).Curated2
Sequence conflicti208 – 209KL → NV in BAA04663 (PubMed:7918659).Curated2
Sequence conflicti263 – 271SIPHMLEHF → QHSAHAGAL in BAA04663 (PubMed:7918659).Curated9

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
D17576 Genomic DNA Translation: BAA04502.1
D21123 Genomic DNA Translation: BAA04663.1
U00096 Genomic DNA Translation: AAC75357.1
AP009048 Genomic DNA Translation: BAA16136.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G65001
JX0357
S50130

NCBI Reference Sequences

More...
RefSeqi
NP_416800.1, NC_000913.3
WP_000086722.1, NZ_STEB01000008.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75357; AAC75357; b2297
BAA16136; BAA16136; BAA16136

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946778

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2294
eco:b2297

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4437

<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
D17576 Genomic DNA Translation: BAA04502.1
D21123 Genomic DNA Translation: BAA04663.1
U00096 Genomic DNA Translation: AAC75357.1
AP009048 Genomic DNA Translation: BAA16136.1
PIRiG65001
JX0357
S50130
RefSeqiNP_416800.1, NC_000913.3
WP_000086722.1, NZ_STEB01000008.1

3D structure databases

SMRiP0A9M8
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4261500, 351 interactors
851119, 1 interactor
DIPiDIP-35815N
IntActiP0A9M8, 28 interactors
STRINGi511145.b2297

2D gel databases

SWISS-2DPAGEiP0A9M8

Proteomic databases

EPDiP0A9M8
jPOSTiP0A9M8
PaxDbiP0A9M8
PRIDEiP0A9M8

Genome annotation databases

EnsemblBacteriaiAAC75357; AAC75357; b2297
BAA16136; BAA16136; BAA16136
GeneIDi946778
KEGGiecj:JW2294
eco:b2297
PATRICifig|1411691.4.peg.4437

Organism-specific databases

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

More...
EchoBASEi
EB4147

Phylogenomic databases

eggNOGiENOG4105C6K Bacteria
COG0280 LUCA
COG0857 LUCA
HOGENOMiHOG000053797
InParanoidiP0A9M8
KOiK13788
PhylomeDBiP0A9M8

Enzyme and pathway databases

UniPathwayiUPA00340;UER00459
BioCyciEcoCyc:PHOSACETYLTRANS-MONOMER
ECOL316407:JW2294-MONOMER
MetaCyc:PHOSACETYLTRANS-MONOMER
BRENDAi2.3.1.8 2026

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0A9M8

Family and domain databases

Gene3Di3.40.1390.20, 1 hit
3.40.50.10750, 1 hit
3.40.50.10950, 1 hit
InterProiView protein in InterPro
IPR010766 DRTGG
IPR016475 P-Actrans_bac
IPR027417 P-loop_NTPase
IPR004614 P_AcTrfase
IPR042113 P_AcTrfase_dom1
IPR042112 P_AcTrfase_dom2
IPR002505 PTA_PTB
IPR028979 Ser_kin/Pase_Hpr-like_N_sf
PfamiView protein in Pfam
PF07085 DRTGG, 1 hit
PF01515 PTA_PTB, 1 hit
PIRSFiPIRSF006107 PhpActrans_proteobac, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF75138 SSF75138, 1 hit
TIGRFAMsiTIGR00651 pta, 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 nameiPTA_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: P0A9M8
Secondary accession number(s): P39184
, P78091, P78189, P78190, Q9EUP2
<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: January 23, 2007
Last modified: November 13, 2019
This is version 120 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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