SECG_METBF
ID SECG_METBF Reviewed; 55 AA.
AC Q46DN2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Mbar_A1042;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000099; AAZ70010.1; -; Genomic_DNA.
DR RefSeq; WP_011306058.1; NC_007355.1.
DR AlphaFoldDB; Q46DN2; -.
DR STRING; 269797.Mbar_A1042; -.
DR EnsemblBacteria; AAZ70010; AAZ70010; Mbar_A1042.
DR GeneID; 3625043; -.
DR KEGG; mba:Mbar_A1042; -.
DR eggNOG; arCOG02957; Archaea.
DR HOGENOM; CLU_208205_1_1_2; -.
DR OMA; AGIMRYF; -.
DR OrthoDB; 128075at2157; -.
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..55
FT /note="Preprotein translocase subunit SecG"
FT /id="PRO_1000046577"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
FT TRANSMEM 30..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
FT TOPO_DOM 52..55
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
SQ SEQUENCE 55 AA; 5781 MW; AADB5FDC68FBE866 CRC64;
MAKKSGSGLQ SSAGLMRYYE ADKNAVQVQP KVVLIVGAIV GIAVLFLSAV NGFWP