(data stored in ACNUC30630 zone)

SWISSPROT: SECA_TROW8

ID   SECA_TROW8              Reviewed;         847 AA.
AC   Q83NT4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   11-DEC-2019, entry version 106.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=TW139;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(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 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}.
DR   EMBL; BX251410; CAD66819.1; -; Genomic_DNA.
DR   RefSeq; WP_011096100.1; NC_004551.1.
DR   SMR; Q83NT4; -.
DR   PRIDE; Q83NT4; -.
DR   EnsemblBacteria; CAD66819; CAD66819; TW139.
DR   GeneID; 29578106; -.
DR   KEGG; tws:TW139; -.
DR   HOGENOM; HOG000218168; -.
DR   KO; K03070; -.
DR   OMA; MVHYDVQ; -.
DR   BioCyc; GCF_000196075:G1EE9-145-MONOMER; -.
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: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; 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; Q83NT4.
DR   SWISS-2DPAGE; Q83NT4.
KW   ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW   Protein transport; Translocation; Transport.
FT   CHAIN           1..847
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000318481"
FT   NP_BIND         102..109
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   847 AA;  94928 MW;  E9DBF5EE8722D41B CRC64;
     MSVKLLERIL RAGEGRTLKR LRNIAHTVNA IEDEYKGCTD GELRTFAFDL KVRHQNGESL
     DSILPEAFAM VREASSRTLG LRHFDVQIMG GAALHMGYIA EMFTGEGKTL VATLPAFLNS
     LSGNGVHIVT VNDYLAGYHS QQMGRVYKVL GLETGVILAD QDPSTRAQQY RADITYGTNN
     EFGFDYLRDN MAWSCAERVQ RGHNFVILDE VDSILIDEAR TPLIISGSSS GEVSRWFVEF
     AGIARALTAG EDYDVDERKH TVGVLEPGIA KVEDLLGISN LYESVNTPLI SFLNNSIKAK
     ELFKRDRDYV VLDGEVMIVD EHTGRILSGR RYNEGLHQAI EAKEGVEIKA ENQTLATVTL
     QNYFRLYKKI SGMTGTAVTE ASEFMSTYKL PVVSIPTNKP NIRKDHPDVV YKNEQIKFEN
     LADHVRECYT RGQPVLIGTT SVEKSEYVSK LLSKRGVRHE VLNAKNHAKE ARIVAEAGRL
     RAVTVATNMA GRGTDIILGG NPEVLTAVEL RRKGLDPSKD PERYEQAWSS AFPKLHRRTR
     EEAEKVIEAG GLMVIGTERH ESRRIDNQLR GRSGRQGDPG ESRFYLSLTD DLMRKFNPGA
     ASALAARVPD DTAIESKLVS RAIRSAQAQV ESLNAETRKN VLKYDDVLNR QRAAIYTDRS
     RILEGGDIAD RVQAFLSDAI EEIINSHAVT AWDFDALWAD LKTIYPVGIS IEELTDEAGG
     MGRITPDFVM REILSDAKFA YEKRESEIGP ESMRDLERKV VLSVIDRCWR DHLYEMEYLK
     EGIGLRAMAQ RDPLVEYQKE GFDMFEAMMG RIREESIGYL FNIDAQVSSN SPSDARNRPI
     EHDDNAV
//

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