ID A0A151BRD5_9ARCH Unreviewed; 58 AA.
AC A0A151BRD5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Preprotein translocase subunit SecG {ECO:0000256|ARBA:ARBA00014522, ECO:0000256|HAMAP-Rule:MF_00751};
DE AltName: Full=Protein transport protein Sec61 subunit beta homolog {ECO:0000256|ARBA:ARBA00031868, ECO:0000256|HAMAP-Rule:MF_00751};
GN Name=secG {ECO:0000256|HAMAP-Rule:MF_00751};
GN ORFNames=AYL33_003560 {ECO:0000313|EMBL:KYH42212.1};
OS Candidatus Bathyarchaeota archaeon B63.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1779372 {ECO:0000313|EMBL:KYH42212.1, ECO:0000313|Proteomes:UP000075614};
RN [1] {ECO:0000313|EMBL:KYH42212.1, ECO:0000313|Proteomes:UP000075614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B63 {ECO:0000313|EMBL:KYH42212.1};
RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT phylum Bathyarchaeota widespread in marine sediments.";
RL Submitted (FEB-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_00751}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162,
CC ECO:0000256|HAMAP-Rule:MF_00751}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004162, ECO:0000256|HAMAP-Rule:MF_00751}.
CC Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the SEC61-beta family.
CC {ECO:0000256|ARBA:ARBA00006103, ECO:0000256|HAMAP-Rule:MF_00751}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYH42212.1}.
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DR EMBL; LUCF01000027; KYH42212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BRD5; -.
DR Proteomes; UP000075614; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_00751};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00751};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_00751};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_00751};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00751};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00751};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00751}.
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00751"
FT TRANSMEM 39..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 58 AA; 6456 MW; 5EA82898CF3AFF5D CRC64;
MSSRRRRRRQ QTAPLPAAGA GLLRFFEEDT PGIRVRPEIV VILAVALIII CIVAQMVV
//
