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Entry version 155 (25 May 2022)
Sequence version 2 (10 Jan 2003)
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Protein

Enterobactin synthase component F

Gene

entF

Organism
Shigella flexneri
Status
Reviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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 the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. EntF catalyzes the activation of L-serine via ATP-dependent PPi exchange reaction to form seryladenylate. Activated L-serine is loaded onto the peptidyl carrier domain via a thioester linkage to the phosphopanthetheine moiety, forming seryl-S-Ppant-EntF. EntF acts then as the sole catalyst for the formation of the three amide and three ester linkages found in enterobactin, using seryladenylate and 2,3-dihydroxybenzoate-S-Ppant-EntB (DHB-S-Ppant-EntB) as substrates, via the formation of a DHB-Ser-S-Ppant-EntF intermediate.

By similarity

<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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pantetheine 4'-phosphateBy similarityNote: Binds 1 phosphopantetheine covalently.By similarity

<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: enterobactin biosynthesis

This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.By similarity
View all proteins of this organism that are known to be involved in the pathway enterobactin biosynthesis and in Siderophore biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei1259Proton acceptor; for thioesterase activityBy similarity1

<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 functionLigase, Multifunctional enzyme, Transferase
Biological processEnterobactin biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00017

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...
ESTHERi
shifl-entf, Thioesterase

<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:
Enterobactin synthase component FBy similarity (EC:6.3.2.14By similarity)
Alternative name(s):
Enterochelin synthase FBy similarity
Nonribosomal peptide synthetase EntFBy similarity
Including the following 1 domains:
L-serine--[L-seryl-carrier protein] ligaseBy similarity (EC:6.2.1.72By similarity)
Alternative name(s):
Serine-activating enzymeBy similarity
Seryl-AMP ligaseBy similarity
<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:entF
Ordered Locus Names:SF0498, S0504
<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>OrganismiShigella flexneri
<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 identifieri623 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
<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
  • UP000002673 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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
  • UP000001006 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

Keywords - Cellular componenti

Cytoplasm

<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 '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_00001930791 – 1281Enterobactin synthase component FAdd BLAST1281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1010O-(pantetheine 4'-phosphoryl)serineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

4'-phosphopantetheine is transferred from CoA to a specific serine of apo-EntF by EntD. Holo-EntF so formed is then acylated with seryl-AMP.By similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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

Proteins EntB, EntD, EntE and EntF are the component of the enterobactin synthase. Components probably do not form a stable complex. EntF acts as a catalytic monomer.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
198214.SF0498

<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

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P29698

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

More...
SMRi
P29698

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini975 – 1050CarrierPROSITE-ProRule annotationAdd BLAST76

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>Regioni1 – 301Elongation/condensationCuratedAdd BLAST301
Regioni486 – 891AdenylationCuratedAdd BLAST406
Regioni1070 – 1281ThioesteraseCuratedAdd BLAST212

<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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000022_2_13_6

Database of Orthologous Groups

More...
OrthoDBi
572620at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.300.30, 1 hit
3.30.559.10, 1 hit
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010071, AA_adenyl_domain
IPR029058, AB_hydrolase
IPR036736, ACP-like_sf
IPR045851, AMP-bd_C_sf
IPR020845, AMP-binding_CS
IPR000873, AMP-dep_Synth/Lig
IPR023213, CAT-like_dom_sf
IPR001242, Condensatn
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR001031, Thioesterase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00501, AMP-binding, 1 hit
PF00668, Condensation, 1 hit
PF00550, PP-binding, 1 hit
PF00975, Thioesterase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00823, PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 1 hit
SSF53474, SSF53474, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01733, AA-adenyl-dom, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00455, AMP_BINDING, 1 hit
PS50075, CARRIER, 1 hit
PS00012, PHOSPHOPANTETHEINE, 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.

P29698-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQHLPLVAA QPGIWMAEKL SDLPSAWSVA HYVELTGEVD APLLARAVVA
60 70 80 90 100
GLAQADTLRM RFTEDNGEVW QWVDDALIFE LPEIIDLRTN IDPHGTAQAL
110 120 130 140 150
MLADLQQDLR VDSGKPLVFH QLIQVADNRW YWYQRYHHLL VDGFSFPAIT
160 170 180 190 200
RQIANIYCAL LRGEPTPASP FTPFADVVEE YQQYRESEAW QRDAAFWVEQ
210 220 230 240 250
RRQLPPPASL SPAPLAGRSA SADILRLKME FTDGEFRQLA TQLSGVQRTD
260 270 280 290 300
LALALTALWL GRLCNRMDYA AGFIFMRRLG SAALTATGPV LNVLPLGIHI
310 320 330 340 350
AAQETLPELA TRLATRLAAQ LKKMRRHQRY DAEQIVRDSG RAAGDEPLFG
360 370 380 390 400
PVLNIKVFDY QLDIPGVQAQ THTLATGPVN DLELALFPDE HGDLSIEILA
410 420 430 440 450
NKQRYDEPTL IQHAERLKML IAQFAADPAL LCGDVDIMLP GEYAQLAQIN
460 470 480 490 500
ATQVEIPETT LSALVAEQAA KTPDAPALAD ARYLFSYREM HEQVVALANL
510 520 530 540 550
LRERGVKPGD SVAVALPRSV FLTLALHAIV EAGAAWLPLD TGYPDDRLKM
560 570 580 590 600
MLEDARPSLL ITTDDQLPRF SDVPNLTNLC YNAPLTPQGS APLQLSQPHH
610 620 630 640 650
TAYIIFTSGS TGRPKGVMVG QTAIVNRLLW MQNHYPLTGE DVVAQKTPCS
660 670 680 690 700
FDVSVWEFFW PFIAGAKLVM AEPEAHRDPL AMQQFFAEYG VTTTHFVPSM
710 720 730 740 750
LAAFVASLTP QTARQSCVTL KQVFCSGEAL PADLCREWQQ LTGAPLHNLY
760 770 780 790 800
GPTEAAVDVS WYPAFGEELA QVRGSSVPIG YPVWNTGLRI LDAMMHPVPP
810 820 830 840 850
GVAGDLYLTG IQLAQGYLGR PDLTASRFIA DPFAPGERMY RTGDVARWLD
860 870 880 890 900
NGAVEYLGRS DDQLKIRGQR IELGEIDRVM QALPDVKQAV THACVINQAA
910 920 930 940 950
ATGGDARQLV GYLVSQSGLP LDTSALQAQL RETLPPHMVP VVLLQLPQLP
960 970 980 990 1000
LSANGKLDRK ALPLPELKAQ APGRAPKAGS ETIIAAAFAS LLGCDVQDAD
1010 1020 1030 1040 1050
ADFFALGGHS LLAMKLAAQL SRQFARQVTP GQVMVASTVA KLATIIDGEE
1060 1070 1080 1090 1100
DSSRRMGFET ILPLREGNGP TLFCFHPASG FAWQFSVLSR YLDPQWSIIG
1110 1120 1130 1140 1150
IQSPRPHGPM QTATNLDEVC EAHLATLLEQ QPHGIAARLR ARGEQVAFLG
1160 1170 1180 1190 1200
LLDTWPPETQ NWQEKEANGL DPEVLAEINR EREAFLAAQQ GSTSTELFTT
1210 1220 1230 1240 1250
IEGNYADAVR LLTTAHSVPF DGKATLFVAE RTLQEGMSPE RAWSPWIAEL
1260 1270 1280
DIYRQDCAHV DIISPGAFVK IGPIIRATLN R
Length:1,281
Mass (Da):140,696
Last modified:January 10, 2003 - 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:i5F1C4AF64E4143C5
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 conflicti1267 – 1269AFV → TFE in M63304 (PubMed:1846151).Curated3

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
AE005674 Genomic DNA Translation: AAN42148.1
AE014073 Genomic DNA Translation: AAP16020.1
M63304 Genomic DNA No translation available.

NCBI Reference Sequences

More...
RefSeqi
NP_706441.1, NC_004337.2
WP_000077741.1, NZ_UDUU01000106.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAN42148; AAN42148; SF0498
AAP16020; AAP16020; S0504

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1023397

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sfl:SF0498
sft:NCTC1_00519
sfx:S0504

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|198214.7.peg.578

<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
AE005674 Genomic DNA Translation: AAN42148.1
AE014073 Genomic DNA Translation: AAP16020.1
M63304 Genomic DNA No translation available.
RefSeqiNP_706441.1, NC_004337.2
WP_000077741.1, NZ_UDUU01000106.1

3D structure databases

AlphaFoldDBiP29698
SMRiP29698
ModBaseiSearch...

Protein-protein interaction databases

STRINGi198214.SF0498

Protein family/group databases

ESTHERishifl-entf, Thioesterase

Genome annotation databases

EnsemblBacteriaiAAN42148; AAN42148; SF0498
AAP16020; AAP16020; S0504
GeneIDi1023397
KEGGisfl:SF0498
sft:NCTC1_00519
sfx:S0504
PATRICifig|198214.7.peg.578

Phylogenomic databases

HOGENOMiCLU_000022_2_13_6
OrthoDBi572620at2

Enzyme and pathway databases

UniPathwayiUPA00017

Family and domain databases

Gene3Di3.30.300.30, 1 hit
3.30.559.10, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR010071, AA_adenyl_domain
IPR029058, AB_hydrolase
IPR036736, ACP-like_sf
IPR045851, AMP-bd_C_sf
IPR020845, AMP-binding_CS
IPR000873, AMP-dep_Synth/Lig
IPR023213, CAT-like_dom_sf
IPR001242, Condensatn
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR001031, Thioesterase
PfamiView protein in Pfam
PF00501, AMP-binding, 1 hit
PF00668, Condensation, 1 hit
PF00550, PP-binding, 1 hit
PF00975, Thioesterase, 1 hit
SMARTiView protein in SMART
SM00823, PKS_PP, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF53474, SSF53474, 1 hit
TIGRFAMsiTIGR01733, AA-adenyl-dom, 1 hit
PROSITEiView protein in PROSITE
PS00455, AMP_BINDING, 1 hit
PS50075, CARRIER, 1 hit
PS00012, PHOSPHOPANTETHEINE, 1 hit

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 nameiENTF_SHIFL
<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: P29698
<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 historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 10, 2003
Last modified: May 25, 2022
This is version 155 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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