ID A0A1I6G6B1_9EURY Unreviewed; 54 AA.
AC A0A1I6G6B1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN04487947_0641 {ECO:0000313|EMBL:SFR37743.1};
OS Halogeometricum rufum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=553469 {ECO:0000313|EMBL:SFR37743.1, ECO:0000313|Proteomes:UP000198531};
RN [1] {ECO:0000313|EMBL:SFR37743.1, ECO:0000313|Proteomes:UP000198531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7736 {ECO:0000313|EMBL:SFR37743.1,
RC ECO:0000313|Proteomes:UP000198531};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOYT01000001; SFR37743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6G6B1; -.
DR STRING; 553469.SAMN04487947_0641; -.
DR OrthoDB; 43651at2157; -.
DR Proteomes; UP000198531; 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..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00751"
FT TRANSMEM 35..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 54 AA; 5618 MW; 6BA026F5F01AA33B CRC64;
MSSGQNSGGL MSSAGLVRYF DAEDRNAIRL DPKSVVAFGL LFGVGVLVLN AVAF
//
