ID   CYSA_BURMA     STANDARD;      PRT;   351 AA.
AC   Q62K82;
DT   01-FEB-2005 (Rel. 46, Created)
DT   01-FEB-2005 (Rel. 46, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Sulfate/thiosulfate import ATP-binding protein cysA (EC 3.6.3.25)
DE   (Sulfate-transporting ATPase).
GN   Name=cysA; OrderedLocusNames=BMA1206;
OS   Burkholderia mallei (Pseudomonas mallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=13373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M.,
RA   Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F.,
RA   Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M.,
RA   Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y.,
RA   Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
CC   -!- FUNCTION: Part of the ABC transporter complex cysAWTP involved in
CC       sulfate/thiosulfate import. Responsible for energy coupling to the
CC       transport system (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + sulfate(Out) = ADP + phosphate +
CC       sulfate(In).
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins
CC       (cysA), two transmembrane proteins (cysT and cysW) and a solute-
CC       binding protein (cysP) (Probable).
CC   -!- SUBCELLULAR LOCATION: Inner membrane-associated (By similarity).
CC   -!- SIMILARITY: Belongs to the ABC transporter family.
CC       Sulfate/tungstate importer (TC 3.A.1.6) subfamily.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; CP000010; AAU47464.1; -.
DR   TIGR; BMA1206; -.
DR   InterPro; IPR003593; AAA_ATPase.
DR   InterPro; IPR003439; ABC_transp_like.
DR   InterPro; IPR000803; Gluc_transporter.
DR   InterPro; IPR008995; MOP_like.
DR   Pfam; PF00005; ABC_tran; 1.
DR   PRINTS; PR00172; GLUCTRNSPORT.
DR   ProDom; PD000006; ABC_transporter; 1.
DR   SMART; SM00382; AAA; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
KW   ATP-binding; Complete proteome; Hydrolase; Inner membrane; Membrane;
KW   Sulfate transport; Transport.
FT   NP_BIND      35     42       ATP (By similarity).
SQ   SEQUENCE   351 AA;  38221 MW;  90F954BACB04498D CRC64;
     MGITVRNLHK RFGEFAALDD VSLDFPAGEL VALLGPSGCG KTTLLRVIAG LEHADSGQVV
     LQGLDVASVG ARERQVGFVF QHYALFRHMT VFENVAFGLR VKPRRERPSE AAIRAKVHEL
     LSLVQLDWLA QRYPSELSGG QRQRIALARA LAVEPKVLLL DEPFGALDAK VRKELRGWLR
     RLHDDLHIST IFVTHDQEEA LEVADRIVVL NHGRVEQVGS PQAVYDHPRS AFVYEFLGAA
     NRLDGTVSGN GFVAHGAAQA IAVDADFAGP ARAYVRPHDL ELAAPHARAQ GIAADVRRVV
     PLGGSVRVEL AARSGEVLEA ELDRNAWRAL ALDVGDALTA VPRAVRVFPA R
//