(data stored in ACNUC7421 zone)

SWISSPROT: D5E3D7_BACMQ

ID   D5E3D7_BACMQ            Unreviewed;       705 AA.
AC   D5E3D7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   SubName: Full=Cadmium-translocating P-type ATPase {ECO:0000313|EMBL:ADE72312.1};
DE            EC=3.6.3.- {ECO:0000313|EMBL:ADE72312.1};
GN   Name=cadA {ECO:0000313|EMBL:ADE72312.1};
GN   OrderedLocusNames=BMQ_pBM40023 {ECO:0000313|EMBL:ADE72312.1};
OS   Bacillus megaterium (strain ATCC 12872 / QMB1551).
OG   Plasmid pBM400 {ECO:0000313|EMBL:ADE72312.1,
OG   ECO:0000313|Proteomes:UP000000935}.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=545693 {ECO:0000313|EMBL:ADE72312.1, ECO:0000313|Proteomes:UP000000935};
RN   [1] {ECO:0000313|EMBL:ADE72312.1, ECO:0000313|Proteomes:UP000000935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935};
RC   PLASMID=Plasmid pBM400 {ECO:0000313|Proteomes:UP000000935};
RX   PubMed=14602653; DOI=10.1128/AEM.69.11.6888-6898.2003;
RA   Scholle M.D., White C.A., Kunnimalaiyaan M., Vary P.S.;
RT   "Sequencing and characterization of pBM400 from Bacillus megaterium QM
RT   B1551.";
RL   Appl. Environ. Microbiol. 69:6888-6898(2003).
RN   [2] {ECO:0000313|Proteomes:UP000000935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935};
RC   PLASMID=Plasmid pBM400 {ECO:0000313|Proteomes:UP000000935};
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J.,
RA   Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J.,
RA   Vary P.S.;
RT   "Genome sequences of the industrial vitamin B12-producers B.
RT   megaterium QM B1551 and DSM319 reveal new insights into the Bacillus
RT   genome evolution and pan-genome structure.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IB subfamily.
CC       {ECO:0000256|RuleBase:RU362081}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|RuleBase:RU362081}.
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DR   EMBL; CP001987; ADE72312.1; -; Genomic_DNA.
DR   RefSeq; WP_011106163.1; NC_004604.2.
DR   EnsemblBacteria; ADE72312; ADE72312; BMQ_pBM40023.
DR   KEGG; bmq:BMQ_pBM40023; -.
DR   HOGENOM; HOG000285828; -.
DR   OMA; MVDFSCA; -.
DR   OrthoDB; 237367at2; -.
DR   Proteomes; UP000000935; Plasmid pBM400.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E3D7.
DR   SWISS-2DPAGE; D5E3D7.
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000935};
KW   Hydrolase {ECO:0000313|EMBL:ADE72312.1};
KW   Membrane {ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Plasmid {ECO:0000313|EMBL:ADE72312.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000935};
KW   Transmembrane {ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    338    360       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    647    666       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    672    693       Helical. {ECO:0000256|RuleBase:RU362081}.
SQ   SEQUENCE   705 AA;  77395 MW;  0433F3AF0B5367F3 CRC64;
     MMMFGVKVAH SLPGRTRFYI PKQLETIHIE TWLRSFPGVY SASYNQVTGS LLIYHHITLS
     LYSLKSFIHK YKHTLKQAAC SWKKAIPIIA CGTIFLVNWY LQRSSYPAIV KALSYWVSTF
     TAIGTSYEVI KDGVIHVLKE RKGNANTLTA ASIFASLYMK NPGSALIITL MSTISELLTD
     YTSEQTKHYI HSVLKLDVSY AWRVKEKGVE EKVLVEDIEV GDKVVVFTGE KIPVDGIIIE
     GNGTADEASI TGEYMPREVS GGDNVYAGSV LQSGHVTVTV EKVGEDTSLS KIVKLLEEAQ
     DKRAPIQNIA DTVAEKMVPV SFGLALLTFF FTRNLNRAMS MLVIDFICGI KLSTATALYA
     SIGRAAKEGA IVKGSDHIEK MSKLNTVILD KTGTITEGTP VVQQVIAAEG FNQEDVIRLA
     AAAEKNSTHP IADAIMKQAK DWNILIPIRD NNAQVETTVG KGISTWLNGK RVIVGSLRFM
     NELKVKTTNL LQHMQNDENV IYVAYDQTLV GVVSIFDKIR SGMHRAVNNL RHQGINDIIM
     LTGDKRTVAR EMARRLKLNW YHAEALPDDK AFYVKKYGRT GAVMMVGDGI NDAPALAHAH
     VGVTMGAKRT DIASEASDVI ITSDNPEMLS ELVGLSKKTM NIIKQNFIAT FAINGIAILF
     GALGIFSPIV GAAIHNAATI GVVINSARIL WLGRETNESQ ILRSA
//

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