(data stored in SCRATCH3701 zone)

SWISSPROT: SECA_VIBVY

ID   SECA_VIBVY              Reviewed;         907 AA.
AC   Q7MNU4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 116.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=VV0621;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC       the SecYEG preprotein conducting channel. Has a central role in
CC       coupling the hydrolysis of ATP to the transfer of proteins into and
CC       across the cell membrane, serving both as a receptor for the
CC       preprotein-SecB complex and as an ATP-driven molecular motor driving
CC       the stepwise translocation of polypeptide chains across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC       Note=May bind 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01382};
CC   -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein
CC       translocation apparatus which comprises SecA, SecYEG and auxiliary
CC       proteins SecDF-YajC and YidC. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC       Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC       50. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01382}.
DR   EMBL; BA000037; BAC93385.1; -; Genomic_DNA.
DR   RefSeq; WP_011149507.1; NC_005139.1.
DR   SMR; Q7MNU4; -.
DR   STRING; 672.VV93_v1c05640; -.
DR   PRIDE; Q7MNU4; -.
DR   EnsemblBacteria; BAC93385; BAC93385; BAC93385.
DR   GeneID; 2623390; -.
DR   KEGG; vvy:VV0621; -.
DR   HOGENOM; HOG000218168; -.
DR   KO; K03070; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01382; SecA; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004027; SEC_C_motif.
DR   InterPro; IPR000185; SecA.
DR   InterPro; IPR020937; SecA_CS.
DR   InterPro; IPR011115; SecA_DEAD.
DR   InterPro; IPR014018; SecA_motor_DEAD.
DR   InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR   InterPro; IPR011116; SecA_Wing/Scaffold.
DR   InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR   InterPro; IPR036670; SecA_X-link_sf.
DR   PANTHER; PTHR30612; PTHR30612; 1.
DR   Pfam; PF02810; SEC-C; 1.
DR   Pfam; PF07517; SecA_DEAD; 1.
DR   Pfam; PF01043; SecA_PP_bind; 1.
DR   Pfam; PF07516; SecA_SW; 1.
DR   PRINTS; PR00906; SECA.
DR   SMART; SM00957; SecA_DEAD; 1.
DR   SMART; SM00958; SecA_PP_bind; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81767; SSF81767; 1.
DR   SUPFAM; SSF81886; SSF81886; 1.
DR   TIGRFAMs; TIGR00963; secA; 1.
DR   PROSITE; PS01312; SECA; 1.
DR   PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7MNU4.
DR   SWISS-2DPAGE; Q7MNU4.
KW   ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW   Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW   Translocation; Transport; Zinc.
FT   CHAIN           1..907
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000321037"
FT   NP_BIND         102..109
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   METAL           891
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   METAL           893
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   METAL           902
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   METAL           903
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   907 AA;  103077 MW;  5FF1D399871C8096 CRC64;
     MITKLLTKVI GSRNDRTLRR LRKIVKEINN YEPTFEALSD EQLKAKTVEF RQRLEQGETL
     DQLLPEAFAT VREASKRVYG MRHFDVQLIG GMVLNAGQIA EMRTGEGKTL TATLPAYLNA
     LAGKGVHIVT VNDYLAKRDA ETNRPLFEFL GMTVGINVPN MPHPAKKEAY QADILYGTNN
     EFGFDYLRDN MAFRNEDRVQ RERFFAVVDE VDSILIDEAR TPLIISGPAE DSSELYTRIN
     ALIPLLQKQD KEDSEEYRGD GHYTVDEKSK QVHLTETGQE FVEELMVKNG LMEEGDTLYS
     PTNISLLHHV NAALRAHVLF EKNVDYIVNE DGEVVIVDEH TGRTMPGRRW SEGLHQAVEA
     KEGVKIQNEN QTLASITFQN YFRLYEKLSG MTGTADTEAF EFQSIYGLET VVIPTNKPMI
     RNDMPDVVYR TEAEKFAAII EDIKARVEKG QPVLVGTVSI EKSELLSNAL KKAKIKHNVL
     NAKFHEKEAE IVAEAGKPGA VTIATNMAGR GTDIVLGGSW QAKVESMANP TQEQIDEIKA
     EWKLVHDQVL ESGGLHIIGT ERHESRRIDN QLRGRSGRQG DAGSSRFYLS MEDSLLRIFT
     SDRMAALIQS GMEEGEAIES KMLSRSIEKA QRKVEGRNFD IRKQLLEYDD VANDQRKVVY
     ELRDELMSVD DISDMIEHNR VDVLQGVIDE YIPPQSLEDM WDLEGLQERL KNDFDIDAPV
     KQWLEEDDKL YEEALREKVI DTAVEVYKAK EEVVGAQVLR NFEKSVMLQT LDTLWKEHLA
     AMDHLRQGIH LRGYAQKNPK QEYKRESFEL FEGLLETLKS DVVMILSKVR VQQQEEVERM
     EAQRRAQAEE AARRAQAQHA SAQSQLADDS DEGHHQPVVR DERKVGRNEP CPCGSGKKYK
     QCHGQIN
//

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