SECG_THEMA
ID SECG_THEMA Reviewed; 67 AA.
AC Q9WYU9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Protein-export membrane protein SecG;
GN Name=secG; OrderedLocusNames=TM_0479;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF SECYEG IN COMPLEX WITH SECA.
RX PubMed=18923516; DOI=10.1038/nature07335;
RA Zimmer J., Nam Y., Rapoport T.A.;
RT "Structure of a complex of the ATPase SecA and the protein-translocation
RT channel.";
RL Nature 455:936-943(2008).
CC -!- FUNCTION: Subunit of the protein translocation channel SecYEG.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of SecY, SecE and SecG subunits. The heterotrimers can form
CC oligomers, although 1 heterotrimer is thought to be able to translocate
CC proteins. Interacts with SecDF, and other proteins may be involved. The
CC channel interacts with SecA via subunit SecY.
CC {ECO:0000269|PubMed:18923516}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the SecG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD35563.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE000512; AAD35563.1; ALT_FRAME; Genomic_DNA.
DR PIR; G72372; G72372.
DR RefSeq; NP_228289.1; NC_000853.1.
DR PDB; 3DIN; X-ray; 4.50 A; E/H=1-67.
DR PDBsum; 3DIN; -.
DR AlphaFoldDB; Q9WYU9; -.
DR SMR; Q9WYU9; -.
DR STRING; 243274.THEMA_02290; -.
DR TCDB; 3.A.5.1.4; the general secretory pathway (sec) family.
DR EnsemblBacteria; AAD35563; AAD35563; TM_0479.
DR KEGG; tma:TM0479; -.
DR PATRIC; fig|243274.5.peg.486; -.
DR eggNOG; COG1314; Bacteria.
DR EvolutionaryTrace; Q9WYU9; -.
DR Proteomes; UP000008183; 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-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..67
FT /note="Protein-export membrane protein SecG"
FT /id="PRO_0000414190"
FT TOPO_DOM 1..14
FT /note="Periplasmic"
FT TRANSMEM 15..29
FT /note="Helical; Name=Helix 1"
FT TOPO_DOM 30..53
FT /note="Cytoplasmic"
FT TRANSMEM 54..63
FT /note="Helical; Name=Helix 2"
FT TOPO_DOM 64..67
FT /note="Periplasmic"
SQ SEQUENCE 67 AA; 7542 MW; 581A6B0E71E23F47 CRC64;
MKTFFLIVHT IISVALIYMV QVQMSKFSEL GGASEVEDFT PFLEEEKAST PVERSLLSCL
YSFSFPA
