ID   CADA_BACPF     STANDARD;      PRT;   723 AA.
AC   P30336;
DT   01-APR-1993 (Rel. 25, Created)
DT   01-APR-1993 (Rel. 25, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Probable cadmium-transporting ATPase (EC 3.6.3.3) (Cadmium efflux
DE   ATPase).
GN   Name=cadA;
OS   Bacillus pseudofirmus.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=79885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OF4;
RX   MEDLINE=92332419; PubMed=1321115;
RA   Ivey D.M., Guffanti A.A., Shen Z., Kudyan N., Krulwich T.A.;
RT   "The cadC gene product of alkaliphilic Bacillus firmus OF4 partially
RT   restores Na+ resistance to an Escherichia coli strain lacking an
RT   Na+/H+ antiporter (NhaA).";
RL   J. Bacteriol. 174:4878-4884(1992).
CC   -!- FUNCTION: This electroneutral antiporter ejects one cadmium ion
CC       while accumulating two protons by an energy-dependent efflux
CC       mechanism.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + Cd(2+)(In) = ADP + phosphate +
CC       Cd(2+)(Out).
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family. Type IB subfamily.
CC   -!- SIMILARITY: Contains 1 HMA domain.
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; M90750; AAA22858.1; -.
DR   PIR; D42707; D42707.
DR   HSSP; P37617; 1MWY.
DR   InterPro; IPR006416; ATPase-IB_hvy.
DR   InterPro; IPR001757; ATPase_E1-E2.
DR   InterPro; IPR001366; Cad_ATPase.
DR   InterPro; IPR005834; Dehal_like_hydro.
DR   InterPro; IPR008250; E1-E2_ATPase_reg.
DR   InterPro; IPR006404; Heavy_met_ATPase.
DR   InterPro; IPR006121; HeavyMe_transpt.
DR   InterPro; IPR006191; Metal_bind.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00941; CDATPASE.
DR   TIGRFAMs; TIGR01512; ATPase-IB2_Cd; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
KW   Antiport; ATP-binding; Cadmium; Cadmium resistance; Hydrolase;
KW   Ion transport; Magnesium; Metal-binding; Phosphorylation;
KW   Transmembrane; Transport.
FT   DOMAIN       13     76       HMA.
FT   ACT_SITE    412    412       4-aspartylphosphate intermediate
FT                                (Probable).
FT   METAL        23     23       Cadmium (Potential).
FT   METAL        26     26       Cadmium (Potential).
SQ   SEQUENCE   723 AA;  78208 MW;  E2A9B1DFF26CC1D9 CRC64;
     MSDQKAITSE QEMKAYRVQG FTCANCAGKF EKNVKQLSGV EDAKVNFGAS KIAVYGNATI
     EELEKAGAFE NLKVTPEKSA RQASQEVKED TKEDKVPFYK KHSTLLYASL LITFGYLSSY
     VNGEENIVTT LLFLASMFIG GLSLFKVGLQ NLLRFEFDMK TLMTVAVIGG AIIGEWAEVA
     IVVILFAISE ALERFSMDRA RQSIRSLMDI APKEALVKRN GQEIMIHVDD IAVGDIMIVK
     PGQKIAMDGV VVSGYSAVNQ TAITGESVPV EKTVDNEVFA GTLNEEGLLE VEITKLVEDT
     TISKIIHLVE EAQGERAPSQ AFVDKFAKYY TPIIMIIATL VAIVPPLFFD GSWETWIYQG
     LAVLVVGCPC ALVISTPISI VSAIGNAAKK GVLVKGGVYL EEMGALKAIA FDKTGTLTKG
     VPAVTDYNVL NKQINEKELL SIITALEYRS QHPLASAIMK KAEEENITYS DVQVEDFSSI
     TGKGIKGIVN GTTYYIGSPK LFKELLTNDF DKDLEQNVTT LQNQGKTAMI IGTEKEILAV
     IAVADEVRES SKEILQKLHQ LGIKKTIMLT GDNKGTANAI GGQVGVSDIE AELMPQDKLD
     FIKQLRSEYG NVAMVGDGVN DAPALAASTV GIAMGGAGTD TALETADVAL MGDDLRKLPS
     TVKLSRKTLN IIKANITFAI AIKFIASLLV IPGWLTLWIA ILSDMGATLL VALNGLRLMR
     VKE
//