(data stored in ACNUC30630 zone)

SWISSPROT: SECA_DEIRA

ID   SECA_DEIRA              Reviewed;         868 AA.
AC   Q9RWU0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
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=DR_0575;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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 as an ATP-driven molecular motor
CC       driving the stepwise translocation of polypeptide chains across the
CC       membrane. {ECO:0000255|HAMAP-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. Other proteins may also be involved.
CC       {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC       {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC       {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01382}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF10155.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AE000513; AAF10155.1; ALT_INIT; Genomic_DNA.
DR   PIR; D75501; D75501.
DR   RefSeq; NP_294298.2; NC_001263.1.
DR   RefSeq; WP_010887220.1; NZ_CP015081.1.
DR   SMR; Q9RWU0; -.
DR   STRING; 243230.DR_0575; -.
DR   EnsemblBacteria; AAF10155; AAF10155; DR_0575.
DR   GeneID; 1798456; -.
DR   KEGG; dra:DR_0575; -.
DR   PATRIC; fig|243230.17.peg.753; -.
DR   eggNOG; ENOG4105CI6; Bacteria.
DR   eggNOG; COG0653; LUCA.
DR   HOGENOM; HOG000218168; -.
DR   InParanoid; Q9RWU0; -.
DR   KO; K03070; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0015462; F:ATPase-coupled protein transmembrane transporter activity; IBA:GO_Central.
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   GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
DR   HAMAP; MF_01382; SecA; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
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; 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; Q9RWU0.
DR   SWISS-2DPAGE; Q9RWU0.
KW   ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW   Protein transport; Reference proteome; Translocation; Transport.
FT   CHAIN           1..868
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000320792"
FT   NP_BIND         100..107
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   868 AA;  97270 MW;  D534956812FF1AE1 CRC64;
     MFRVLNKVFD NNKRDVERII QTVVKPVNAL EEETMRVENL AEAFMDLRRR VQDGGESLDS
     LIVPAFALIR EAGRRSIGKR HYDTQLIGGA ALHQGRIAEM RTGEGKTLVA TLALAFNALE
     GKGCHLVTVN DYLARVGMEE MGLLYRTLGL TVGLANRELS PAEKQAAYAC DITYVTNSEL
     GFDYLRDNMA QSKEALVLRA DTPLHYAIVD EVDSILIDEA RTPLIISGAA EKATDLYYVF
     AKLIRRLQKG EPAEPGVRTE PTGDYTIEEK SKAVHLTEQG ITKIERLLSL KDLYSPENMD
     KAHMITQAIR ARELYHREKD YIVNAEGEVV IVDEFTGRSM PGRRYGEGLH QAIEAKEGVK
     IENENQTLAT ITYQNFFRLY DKFAGMTGTA KTEEKEFLDI YGSDVLVIPT NKPVIRVDSD
     DLIYRTRMGK YAAVVGEVQE MHATGRPILI GTASIETSEQ LSSLLQQAGV QHAVLNAKFE
     AQEASIIAQA GRSGTVTIAT NMAGRGTDIM LGGNDEYIIG ESIEQQLGVS RYAPEVEAFI
     KAISREDPAA EQLGMQIPGI TLDFIRQAQE LHRATVEDRQ RVRDLGGLHI VGTERHESRR
     IDNQLRGRAG RQGDPGSSRF YVSFEDDLMR LFANDRVVGM MDRLGMDDSQ PIEAKMVTGA
     IEKAQARVED RNFGIRKQLL EFDNVMSKQR DEIYAQRREV LLGPDEDIEE TTEGMIGDFV
     DSQLAAYAPI EVSHEQWDIE QLRSAMVEAV PALETFDFES LRVNSPAEAQ DRLLSAVADA
     FDARKEELSP TMMNSLARYV LLQVVDQHWK EHLHGMDVLR QGIGLRGYGQ RDPFTEYKFE
     ATNMFNEMID ALKADVTKFI FRMQFGGA
//

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