ID   SECG_SULAC              Reviewed;          59 AA.
AC   P60464; Q4JAS2;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Preprotein translocase subunit SecG;
DE   AltName: Full=Protein transport protein Sec61 subunit beta homolog;
GN   OrderedLocusNames=Saci_0729;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7688716; DOI=10.1128/jb.175.16.5043-5048.1993;
RA   LaGrandeur T.E., Darr S.C., Haas E.S., Pace N.R.;
RT   "Characterization of the RNase P RNA of Sulfolobus acidocaldarius.";
RL   J. Bacteriol. 175:5043-5048(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SEC61-beta family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=L13597; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L13597; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   EMBL; CP000077; AAY80107.1; -; Genomic_DNA.
DR   RefSeq; WP_011277609.1; NC_007181.1.
DR   AlphaFoldDB; P60464; -.
DR   SMR; P60464; -.
DR   STRING; 330779.Saci_0729; -.
DR   EnsemblBacteria; AAY80107; AAY80107; Saci_0729.
DR   GeneID; 3473261; -.
DR   KEGG; sai:Saci_0729; -.
DR   PATRIC; fig|330779.12.peg.698; -.
DR   eggNOG; arCOG02957; Archaea.
DR   HOGENOM; CLU_208205_2_1_2; -.
DR   OMA; RYYEEEH; -.
DR   Proteomes; UP000001018; 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..59
FT                   /note="Preprotein translocase subunit SecG"
FT                   /id="PRO_0000157278"
FT   TOPO_DOM        1..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..59
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   59 AA;  6366 MW;  10FE4FFDEFB3A7C0 CRC64;
     MPSSKKKKED VPIASMAGLV RYYESEKEKV KISPKVVVVA SIVLIAGVII ASFIIPPPL