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Entry version 137 (07 Apr 2021)
Sequence version 1 (01 Feb 1997)
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Protein

Ancillary SecYEG translocon subunit

Gene

yfgM

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

May mediate protein transfer from the SecYEG translocon to the periplasmic chaperone network via its periplasmic C-terminal region (PubMed:24855643). In addition, at the cytosolic site, acts as a negative regulator of RcsB (PubMed:26092727). In stationary phase, the FtsH-dependent degradation of YfgM ensures the release of RcsB from YfgM and thereby permits cellular protection by the Rcs phosphorelay system (PubMed:26092727). May coordinate stress responses across the inner membrane via a dynamic protein-protein interaction network inside and outside of the membrane (PubMed:26092727).2 Publications

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

Is stable during exponential growth and degraded in stationary phase by the essential FtsH protease. Degradation is influenced by the alarmone (p)ppGpp, but not by inorganic polyphosphate (polyP), RpoS, RcsB or PpiD.1 Publication

<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

<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 functionChaperone

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G7321-MONOMER

<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:
Ancillary SecYEG translocon subunitCurated
Alternative name(s):
Periplasmic chaperone YfgM1 Publication
<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:yfgM
Ordered Locus Names:b2513, JW2497
<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 domaini1 – 23Cytoplasmic1 PublicationAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei24 – 43HelicalSequence analysisAdd BLAST20
Topological domaini44 – 206Periplasmic1 PublicationAdd BLAST163

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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

Deletion of the gene in combination with either surA or skp causes increased sensitivity to vancomycin and exacerbates the RpoE-dependent envelope stress response in a skp deletion strain (PubMed:24855643). Strains lacking the gene show a decreased survival rate at low pH (PubMed:25403562). Several cell envelope proteins are misfolded/mistargeted and turned-over in the absence of YfgM, including HdeB and AnsB (PubMed:25403562).2 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>Mutagenesisi2 – 3Missing : Is able to insert into the inner membrane but is no longer degraded in stationary growth phase. 1 Publication2
Mutagenesisi2E → A, K or Q: Stable under all growth conditions. 1 Publication1
Mutagenesisi2E → D: Decreases degradation by FtsH. 1 Publication1
Mutagenesisi3I → A: Stable under all growth conditions. 1 Publication1
Mutagenesisi4Y → A: Destabilizes the protein, which is prone to degradation in early or late exponential phase. 1 Publication1
Mutagenesisi5E → A: Destabilizes the protein, which is prone to degradation in early or late exponential phase. 1 Publication1
Mutagenesisi6N → A: Decreases degradation by FtsH. 1 Publication1
Mutagenesisi7E → A: Decreases degradation by FtsH. 1 Publication1
Mutagenesisi8N → A: Decreases degradation by FtsH. 1 Publication1
Mutagenesisi9D → A: Decreases degradation by FtsH. 1 Publication1
Mutagenesisi10Q → A: Decreases degradation by FtsH. 1 Publication1
Mutagenesisi11V → D: Decreases degradation by FtsH. 1 Publication1
Mutagenesisi12E → A: Decreases degradation by FtsH. 1 Publication1
Mutagenesisi13A → D: Decreases degradation by FtsH. 1 Publication1
Mutagenesisi14V → D: Decreases degradation by FtsH. 1 Publication1
Mutagenesisi15K → A: Does not affect degradation by FtsH. 1 Publication1
Mutagenesisi16R → A: Does not affect degradation by FtsH. 1 Publication1
Mutagenesisi17F → A: Does not affect degradation by FtsH. 1 Publication1
Mutagenesisi18F → A: Does not affect degradation by FtsH. 1 Publication1

<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_00002143641 – 206Ancillary SecYEG translocon subunitAdd BLAST206

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P76576

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

More...
PaxDbi
P76576

PRoteomics IDEntifications database

More...
PRIDEi
P76576

<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

Interacts with the SecYEG translocon (PubMed:24855643, PubMed:31699901).

Forms a complex with PpiD (PubMed:21210718, PubMed:24855643, PubMed:31699901).

Also interacts with RcsB (PubMed:26092727).

4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260588, 38 interactors
851320, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-12043N

Protein interaction database and analysis system

More...
IntActi
P76576, 5 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2513

<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
P76576

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

<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 first 14 N-terminal residues form the YfgM degron, which directs the protein to FtsH for proteolysis.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

Belongs to the YfgM family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2976, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_084785_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P76576

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011990, TPR-like_helical_dom_sf
IPR018704, TPR_21
IPR026039, UPF0070

The PANTHER Classification System

More...
PANTHERi
PTHR38035, PTHR38035, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF09976, TPR_21, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF006170, YfgM, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48452, SSF48452, 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.

P76576-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEIYENENDQ VEAVKRFFAE NGKALAVGVI LGVGALIGWR YWNSHQVDSA
60 70 80 90 100
RSASLAYQNA VTAVSEGKPD SIPAAEKFAA ENKNTYGALA SLELAQQFVD
110 120 130 140 150
KNELEKAAAQ LQQGLADTSD ENLKAVINLR LARVQVQLKQ ADAALKTLDT
160 170 180 190 200
IKGEGWAAIV ADLRGEALLS KGDKQGARSA WEAGVKSDVT PALSEMMQMK

INNLSI
Length:206
Mass (Da):22,176
Last modified:February 1, 1997 - 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:i2DAFC595EBDC5EEB
GO

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
U00096 Genomic DNA Translation: AAC75566.1
AP009048 Genomic DNA Translation: BAA16399.2

Protein sequence database of the Protein Information Resource

More...
PIRi
H65027

NCBI Reference Sequences

More...
RefSeqi
NP_417008.1, NC_000913.3
WP_000409205.1, NZ_STEB01000011.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75566; AAC75566; b2513
BAA16399; BAA16399; BAA16399

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
57732385
946981

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2497
eco:b2513

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.2612

<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
U00096 Genomic DNA Translation: AAC75566.1
AP009048 Genomic DNA Translation: BAA16399.2
PIRiH65027
RefSeqiNP_417008.1, NC_000913.3
WP_000409205.1, NZ_STEB01000011.1

3D structure databases

SMRiP76576
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi4260588, 38 interactors
851320, 1 interactor
DIPiDIP-12043N
IntActiP76576, 5 interactors
STRINGi511145.b2513

Proteomic databases

jPOSTiP76576
PaxDbiP76576
PRIDEiP76576

Genome annotation databases

EnsemblBacteriaiAAC75566; AAC75566; b2513
BAA16399; BAA16399; BAA16399
GeneIDi57732385
946981
KEGGiecj:JW2497
eco:b2513
PATRICifig|511145.12.peg.2612

Organism-specific databases

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

More...
EchoBASEi
EB3961

Phylogenomic databases

eggNOGiCOG2976, Bacteria
HOGENOMiCLU_084785_0_0_6
InParanoidiP76576

Enzyme and pathway databases

BioCyciEcoCyc:G7321-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P76576

Family and domain databases

Gene3Di1.25.40.10, 1 hit
InterProiView protein in InterPro
IPR011990, TPR-like_helical_dom_sf
IPR018704, TPR_21
IPR026039, UPF0070
PANTHERiPTHR38035, PTHR38035, 1 hit
PfamiView protein in Pfam
PF09976, TPR_21, 1 hit
PIRSFiPIRSF006170, YfgM, 1 hit
SUPFAMiSSF48452, SSF48452, 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 nameiYFGM_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: P76576
Secondary accession number(s): P76982, P76983
<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: December 15, 1998
Last sequence update: February 1, 1997
Last modified: April 7, 2021
This is version 137 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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