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SECG_PYRIL
ID   SECG_PYRIL              Reviewed;          57 AA.
AC   A1RVP5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=Pisl_1880;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000504; ABL89027.1; -; Genomic_DNA.
DR   RefSeq; WP_011763602.1; NC_008701.1.
DR   AlphaFoldDB; A1RVP5; -.
DR   SMR; A1RVP5; -.
DR   STRING; 384616.Pisl_1880; -.
DR   EnsemblBacteria; ABL89027; ABL89027; Pisl_1880.
DR   GeneID; 4616526; -.
DR   KEGG; pis:Pisl_1880; -.
DR   eggNOG; arCOG02957; Archaea.
DR   HOGENOM; CLU_208205_2_1_2; -.
DR   OrthoDB; 131825at2157; -.
DR   Proteomes; UP000002595; 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; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..57
FT                   /note="Preprotein translocase subunit SecG"
FT                   /id="PRO_1000046582"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
FT   TRANSMEM        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
FT   TOPO_DOM        56..57
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
SQ   SEQUENCE   57 AA;  6412 MW;  93838B827D05AE8B CRC64;
     MARRRKYEGL NPFVAAGLIK FSEEGELERI KLNPRTAILV SITVIIAILV LNILHPL
 
 
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