SECG_METBU
ID SECG_METBU Reviewed; 58 AA.
AC Q12U86;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=Mbur_2117;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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; CP000300; ABE52990.1; -; Genomic_DNA.
DR RefSeq; WP_011500129.1; NC_007955.1.
DR AlphaFoldDB; Q12U86; -.
DR SMR; Q12U86; -.
DR STRING; 259564.Mbur_2117; -.
DR EnsemblBacteria; ABE52990; ABE52990; Mbur_2117.
DR GeneID; 3998200; -.
DR KEGG; mbu:Mbur_2117; -.
DR HOGENOM; CLU_208205_1_1_2; -.
DR OMA; AGIMRYF; -.
DR OrthoDB; 128075at2157; -.
DR Proteomes; UP000001979; 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_1000133344"
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; 6140 MW; B5A3E03A8745387F CRC64;
MAQKKKSSGS GLMSSAGLMT YYDADKKAIH VQPKTVFIFG AICGIVILAF SAGFGLWP