YFGM_BUCBP
ID YFGM_BUCBP Reviewed; 193 AA.
AC Q89A13;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ancillary SecYEG translocon subunit {ECO:0000250|UniProtKB:P76576};
DE AltName: Full=Chaperone YfgM {ECO:0000250|UniProtKB:P76576};
GN OrderedLocusNames=bbp_550;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC -!- FUNCTION: May mediate protein transfer from the Sec translocon to the
CC chaperone network via its extracellular C-terminal region.
CC {ECO:0000250|UniProtKB:P76576}.
CC -!- SUBUNIT: Interacts with the Sec translocon (By similarity). Forms a
CC complex with PpiD (By similarity). {ECO:0000250|UniProtKB:P76576}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P76576};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:P76576};
CC Extracellular side {ECO:0000250|UniProtKB:P76576}.
CC -!- SIMILARITY: Belongs to the YfgM family. {ECO:0000305}.
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DR EMBL; AE016826; AAO27248.1; -; Genomic_DNA.
DR RefSeq; WP_011091649.1; NC_004545.1.
DR AlphaFoldDB; Q89A13; -.
DR SMR; Q89A13; -.
DR STRING; 224915.bbp_550; -.
DR EnsemblBacteria; AAO27248; AAO27248; bbp_550.
DR GeneID; 56471084; -.
DR KEGG; bab:bbp_550; -.
DR eggNOG; COG2976; Bacteria.
DR HOGENOM; CLU_084785_0_1_6; -.
DR OMA; GMAENIR; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR018704; TPR_21.
DR InterPro; IPR026039; YfgM.
DR PANTHER; PTHR38035; PTHR38035; 1.
DR Pfam; PF09976; TPR_21; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 3: Inferred from homology;
KW Cell membrane; Chaperone; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..193
FT /note="Ancillary SecYEG translocon subunit"
FT /id="PRO_0000214363"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P76576"
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..193
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P76576"
SQ SEQUENCE 193 AA; 22850 MW; 12ADB4A6846885A3 CRC64;
MIKNSYINEK LNFYQKSFLT CMLLIVIVIV YFFSKNYLDK PKNSYVHTKM MTFLTNSNEL
NISKNLIWTK KTISGNLMSL KLAKVYVINN QLEKALKILE KSKNNSVDLN FFNLISFKIA
QIYFQKNNIK KAITTIKDIL GDSWDSIRNN FIGDVYFKLD NQKRAVTLWK RSIIQNKKIE
FEKIIQMKIN NYN