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Entry version 128 (02 Jun 2021)
Sequence version 2 (23 Jan 2007)
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Protein

Elongation factor P

Gene

efp

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 peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Beta-lysylation at Lys-34 is required for alleviation. The Pro codons and their context do not affect activity; only consecutive Pro residues (not another amino acid) are affected by EF-P. Has stimulatory effects on peptide bond formation between ribosome-bound initiator tRNA(fMet) and puromycin, and N-acetyl-Phe tRNA(Phe)-primed poly(U)-directed poly(Phe) synthesis.

2 Publications

Caution

The modification on Lys-34 was initially thought to be a spermidine residue.1 Publication

<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: polypeptide chain elongation

This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.
View all proteins of this organism that are known to be involved in the pathway polypeptide chain elongation and in Protein 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 functionElongation factor
Biological processProtein biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG12099-MONOMER
MetaCyc:EG12099-MONOMER

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

More...
UniPathwayi
UPA00345

<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:
Elongation factor P
Short name:
EF-P
<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:efp
Ordered Locus Names:b4147, JW4107
<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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • 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

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

Disruption of this gene leads to lethality (PubMed:9405429) or to a very slow growth phenotype (PubMed:20729861). Required for the expression of poly-Pro-containing proteins.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi31K → A: No lysylation. 1 Publication1
Mutagenesisi33G → K: No lysylation. Loss of in vivo EF-P function for cell growth. 1 Publication1
Mutagenesisi34K → A: No lysylation and loss of EF-P activity. No facilitation of translation of poly-Pro stretches. 3 Publications1

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000942452 – 188Elongation factor PAdd BLAST187

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 residuei34N6-(3,6-diaminohexanoyl)-5-hydroxylysine3 Publications1

<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

Is beta-lysylated on the epsilon-amino group of Lys-34 by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC. Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety would extend toward the peptidyltransferase center and stabilize the terminal 3-CCA end of the tRNA. The hydroxylation of the C5 position on Lys-34 would allow additional potential stabilizing hydrogen-bond interactions with the P-tRNA (PubMed:21841797 PubMed:22128152 PubMed:22706199 and PubMed:20729861).3 Publications

Keywords - PTMi

Hydroxylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A6N4

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

More...
PaxDbi
P0A6N4

PRoteomics IDEntifications database

More...
PRIDEi
P0A6N4

<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

Binds 30S, 50S and 70S ribosomes, possibly near the A site, note that T.thermophilus structures show binding between the P and E sites (PDB 3HUW and 3HUY). Proportionally less EF-P binds to larger polysomes, suggesting it has a role early in translation. It is present in 1 copy per 10 ribosomes.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260776, 791 interactors

Database of interacting proteins

More...
DIPi
DIP-31834N

Protein interaction database and analysis system

More...
IntActi
P0A6N4, 1 interactor

STRING: functional protein association networks

More...
STRINGi
511145.b4147

<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

1188
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
P0A6N4

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

<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 elongation factor P family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0231, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_074944_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A6N4

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A6N4

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04470, S1_EF-P_repeat_1, 1 hit
cd05794, S1_EF-P_repeat_2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.30.30, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00141, EF_P, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015365, Elong-fact-P_C
IPR012340, NA-bd_OB-fold
IPR014722, Rib_L2_dom2
IPR020599, Transl_elong_fac_P/YeiP
IPR013185, Transl_elong_KOW-like
IPR001059, Transl_elong_P/YeiP_cen
IPR013852, Transl_elong_P/YeiP_CS
IPR011768, Transl_elongation_fac_P
IPR008991, Translation_prot_SH3-like_sf

The PANTHER Classification System

More...
PANTHERi
PTHR30053, PTHR30053, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01132, EFP, 1 hit
PF08207, EFP_N, 1 hit
PF09285, Elong-fact-P_C, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005901, EF-P, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01185, EFP, 1 hit
SM00841, Elong-fact-P_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50104, SSF50104, 1 hit
SSF50249, SSF50249, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00038, efp, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01275, EFP, 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.

<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 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.

P0A6N4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATYYSNDFR AGLKIMLDGE PYAVEASEFV KPGKGQAFAR VKLRRLLTGT
60 70 80 90 100
RVEKTFKSTD SAEGADVVDM NLTYLYNDGE FWHFMNNETF EQLSADAKAI
110 120 130 140 150
GDNAKWLLDQ AECIVTLWNG QPISVTPPNF VELEIVDTDP GLKGDTAGTG
160 170 180
GKPATLSTGA VVKVPLFVQI GEVIKVDTRS GEYVSRVK
Length:188
Mass (Da):20,591
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:iE36E136D4399460F
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 20591.6 Da. Determined by ESI. With N6-(3,6-diaminohexanoyl)-5-hydroxy-Lys-34.1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X61676 Genomic DNA Translation: CAA43851.1
U14003 Genomic DNA Translation: AAA97046.1
U00096 Genomic DNA Translation: AAC77107.1
AP009048 Genomic DNA Translation: BAE78149.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S34443

NCBI Reference Sequences

More...
RefSeqi
NP_418571.1, NC_000913.3
WP_000257278.1, NZ_STEB01000014.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC77107; AAC77107; b4147
BAE78149; BAE78149; BAE78149

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
61753799
948661

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW4107
eco:b4147

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2553

<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
X61676 Genomic DNA Translation: CAA43851.1
U14003 Genomic DNA Translation: AAA97046.1
U00096 Genomic DNA Translation: AAC77107.1
AP009048 Genomic DNA Translation: BAE78149.1
PIRiS34443
RefSeqiNP_418571.1, NC_000913.3
WP_000257278.1, NZ_STEB01000014.1

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
3A5ZX-ray2.50B/D/F/H1-188[»]
6ENJelectron microscopy3.70w1-188[»]
6ENUelectron microscopy3.10w1-188[»]
SMRiP0A6N4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260776, 791 interactors
DIPiDIP-31834N
IntActiP0A6N4, 1 interactor
STRINGi511145.b4147

Proteomic databases

jPOSTiP0A6N4
PaxDbiP0A6N4
PRIDEiP0A6N4

Genome annotation databases

EnsemblBacteriaiAAC77107; AAC77107; b4147
BAE78149; BAE78149; BAE78149
GeneIDi61753799
948661
KEGGiecj:JW4107
eco:b4147
PATRICifig|1411691.4.peg.2553

Organism-specific databases

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

More...
EchoBASEi
EB2023

Phylogenomic databases

eggNOGiCOG0231, Bacteria
HOGENOMiCLU_074944_0_0_6
InParanoidiP0A6N4
PhylomeDBiP0A6N4

Enzyme and pathway databases

UniPathwayiUPA00345
BioCyciEcoCyc:EG12099-MONOMER
MetaCyc:EG12099-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0A6N4

Family and domain databases

CDDicd04470, S1_EF-P_repeat_1, 1 hit
cd05794, S1_EF-P_repeat_2, 1 hit
Gene3Di2.30.30.30, 1 hit
HAMAPiMF_00141, EF_P, 1 hit
InterProiView protein in InterPro
IPR015365, Elong-fact-P_C
IPR012340, NA-bd_OB-fold
IPR014722, Rib_L2_dom2
IPR020599, Transl_elong_fac_P/YeiP
IPR013185, Transl_elong_KOW-like
IPR001059, Transl_elong_P/YeiP_cen
IPR013852, Transl_elong_P/YeiP_CS
IPR011768, Transl_elongation_fac_P
IPR008991, Translation_prot_SH3-like_sf
PANTHERiPTHR30053, PTHR30053, 1 hit
PfamiView protein in Pfam
PF01132, EFP, 1 hit
PF08207, EFP_N, 1 hit
PF09285, Elong-fact-P_C, 1 hit
PIRSFiPIRSF005901, EF-P, 1 hit
SMARTiView protein in SMART
SM01185, EFP, 1 hit
SM00841, Elong-fact-P_C, 1 hit
SUPFAMiSSF50104, SSF50104, 1 hit
SSF50249, SSF50249, 2 hits
TIGRFAMsiTIGR00038, efp, 1 hit
PROSITEiView protein in PROSITE
PS01275, EFP, 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 nameiEFP_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: P0A6N4
Secondary accession number(s): P33398, Q2M6F7
<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: May 10, 2005
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 128 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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