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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
 
 
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