ID   SECG_IGNH4              Reviewed;          58 AA.
AC   A8ABD7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=Igni_1061;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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; CP000816; ABU82239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8ABD7; -.
DR   SMR; A8ABD7; -.
DR   STRING; 453591.Igni_1061; -.
DR   EnsemblBacteria; ABU82239; ABU82239; Igni_1061.
DR   KEGG; iho:Igni_1061; -.
DR   eggNOG; arCOG02957; Archaea.
DR   HOGENOM; CLU_208205_2_1_2; -.
DR   Proteomes; UP000000262; 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..58
FT                   /note="Preprotein translocase subunit SecG"
FT                   /id="PRO_1000046576"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
FT   TRANSMEM        33..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
FT   TOPO_DOM        55..58
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
SQ   SEQUENCE   58 AA;  6312 MW;  1E3FD6534FF3BF48 CRC64;
     MARKRRKGGE GLVTAIGLVR FYEEVEEKIK VPPEAVIGAA FALSIMTIAL DLLLKAAR