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SECG_METST
ID   SECG_METST              Reviewed;          56 AA.
AC   Q2NHI7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Preprotein translocase subunit SecG {ECO:0000255|HAMAP-Rule:MF_00751};
DE   AltName: Full=Protein transport protein Sec61 subunit beta homolog {ECO:0000255|HAMAP-Rule:MF_00751};
GN   Name=secG {ECO:0000255|HAMAP-Rule:MF_00751}; OrderedLocusNames=Msp_0229;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
CC   -!- FUNCTION: Involved in protein export. The function of the beta subunit
CC       is unknown, but it may be involved in stabilization of the trimeric
CC       complex. {ECO:0000255|HAMAP-Rule:MF_00751}.
CC   -!- SUBUNIT: Component of the protein translocase complex. Heterotrimer
CC       consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. Can
CC       form oligomers of the heterotrimer. {ECO:0000255|HAMAP-Rule:MF_00751}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00751};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00751}.
CC   -!- SIMILARITY: Belongs to the SEC61-beta family. {ECO:0000255|HAMAP-
CC       Rule:MF_00751}.
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DR   EMBL; CP000102; ABC56646.1; -; Genomic_DNA.
DR   RefSeq; WP_011405845.1; NC_007681.1.
DR   AlphaFoldDB; Q2NHI7; -.
DR   SMR; Q2NHI7; -.
DR   STRING; 339860.Msp_0229; -.
DR   EnsemblBacteria; ABC56646; ABC56646; Msp_0229.
DR   GeneID; 41324802; -.
DR   KEGG; mst:Msp_0229; -.
DR   eggNOG; arCOG02957; Archaea.
DR   HOGENOM; CLU_208205_3_1_2; -.
DR   OMA; EQVVIMT; -.
DR   OrthoDB; 128075at2157; -.
DR   Proteomes; UP000001931; 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:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00751; SecG; 1.
DR   InterPro; IPR023531; Preprot_translocase_SecG.
DR   InterPro; IPR016482; SecG/Sec61-beta/Sbh.
DR   Pfam; PF03911; Sec61_beta; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Protein transport; Reference proteome;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..56
FT                   /note="Preprotein translocase subunit SecG"
FT                   /id="PRO_1000046578"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
FT   TRANSMEM        31..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
FT   TOPO_DOM        53..56
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
SQ   SEQUENCE   56 AA;  5969 MW;  3E408E8ACC0C14BA CRC64;
     MARKDKKTLP ASGAGIVRYF NDDTAGVKLS PKQVVIGTII VALICIALRF TTSVGY
 
 
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