SECG_AQUAE
ID SECG_AQUAE Reviewed; 100 AA.
AC O66505;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein-export membrane protein SecG;
GN Name=secG; OrderedLocusNames=aq_098;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (7.5 ANGSTROMS) OF SECYEG IN COMPLEX WITH B.SUBTILIS
RP 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 {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SecG family. {ECO:0000305}.
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DR EMBL; AE000657; AAC06462.1; -; Genomic_DNA.
DR PIR; F70309; F70309.
DR RefSeq; NP_213064.1; NC_000918.1.
DR RefSeq; WP_010880002.1; NC_000918.1.
DR PDB; 3DL8; X-ray; 7.50 A; E/F=1-100.
DR PDBsum; 3DL8; -.
DR AlphaFoldDB; O66505; -.
DR SMR; O66505; -.
DR DIP; DIP-59811N; -.
DR IntAct; O66505; 2.
DR STRING; 224324.aq_098; -.
DR PRIDE; O66505; -.
DR EnsemblBacteria; AAC06462; AAC06462; aq_098.
DR KEGG; aae:aq_098; -.
DR eggNOG; COG1314; Bacteria.
DR HOGENOM; CLU_094156_2_2_0; -.
DR InParanoid; O66505; -.
DR OMA; YWLGGIF; -.
DR OrthoDB; 2225470at2; -.
DR EvolutionaryTrace; O66505; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
DR InterPro; IPR004692; SecG.
DR PANTHER; PTHR34182; PTHR34182; 1.
DR Pfam; PF03840; SecG; 1.
DR PRINTS; PR01651; SECGEXPORT.
DR TIGRFAMs; TIGR00810; secG; 1.
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..100
FT /note="Protein-export membrane protein SecG"
FT /id="PRO_0000157219"
FT TOPO_DOM 1..7
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..32
FT /note="Helical; Name=1"
FT TOPO_DOM 33..48
FT /note="Cytoplasmic"
FT TRANSMEM 49..70
FT /note="Helical; Name=2"
FT TOPO_DOM 71..100
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT REGION 77..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 100 AA; 10464 MW; C7183A51B27FA21A CRC64;
MYYALLTLFV IIAVVLIIST LLQKGRGDVG AAFGGGMGQS IFGVGGVETI LTKATYWLGA
LFLVLALLLS VIPKEKGSVV EKSVQTEQSE GKGTTQESGK