(data stored in ACNUC7421 zone)

SWISSPROT: D6XWM7_BACIE

ID   D6XWM7_BACIE            Unreviewed;       717 AA.
AC   D6XWM7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ADH97869.1};
GN   OrderedLocusNames=Bsel_0329 {ECO:0000313|EMBL:ADH97869.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97869.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97869.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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|PROSITE-ProRule:PRU00280}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001791; ADH97869.1; -; Genomic_DNA.
DR   STRING; 439292.Bsel_0329; -.
DR   EnsemblBacteria; ADH97869; ADH97869; Bsel_0329.
DR   KEGG; bse:Bsel_0329; -.
DR   eggNOG; ENOG4105C59; Bacteria.
DR   eggNOG; COG2217; LUCA.
DR   HOGENOM; HOG000250399; -.
DR   KO; K01534; -.
DR   OMA; NNEMYYV; -.
DR   BioCyc; BSEL439292:G1GLR-354-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
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   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   CDD; cd00371; HMA; 1.
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; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   Pfam; PF00403; HMA; 1.
DR   PRINTS; PR00941; CDATPASE.
DR   SUPFAM; SSF55008; SSF55008; 1.
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.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XWM7.
DR   SWISS-2DPAGE; D6XWM7.
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Membrane {ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Selenium {ECO:0000313|EMBL:ADH97869.1};
KW   Selenocysteine {ECO:0000313|EMBL:ADH97869.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM     99    116       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    320    338       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    350    379       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    661    681       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   DOMAIN       16     79       HMA. {ECO:0000259|PROSITE:PS50846}.
FT   NON_STD      26     26       Selenocysteine. {ECO:0000313|EMBL:
FT                                ADH97869.1}.
SQ   SEQUENCE   717 AA;  76623 MW;  727D2C3BD3AB8484 CRC64;
     MGERKLDDQQ SVADSTATYR IDGLSUADCA KTFESNVKRL DGVEDANLNF GAAKITVSGH
     TTIKELEKAG AFEGLKLRPE RASSSKQVSF WKLPTTRKVY VATLLLLVAL AATVQYGESH
     PVTGIAYLAT VITGGYSLFN KGFRNLIRLN FDMNTLMTIA VTGAAIIGEW MEGAIVVILF
     AISEALERYS MDKARQSIAS LMDIAPNEAL IRRNGEERML LVEDIQVGDI MIVKPGEKLA
     MDGRVVSGTS SINQAAITGE SVPVMKDSGD DVFAGTLNEE GLLEIEVTRL VEDTTLAKII
     HLVEEAQNEQ APSQQFVDRF AYYYTPAIIV LAALVMTVPP LVTGAPWETW IYLGLATLVV
     GCPCALVIST PVAVVTAIGN AARNGVLIKG GIHLEEAGGL KAMAFDKTGT LTKGTPVVTD
     VIPFAYGKEE ALHLAAAVED GSKHPLATAI IRAAEASGFD RSAYVMSGFR SLTSLGVEAS
     VNGETILTGS PRVFQDRGLL HDERIQETIA SLEASGKTVM AVGHSTALIA LIAVADEVRE
     TAKSVIKDLN RMAIETVMLT GDNERTANAI AHDTGVTRVY AGLMPEDKLD RIRNLRHSHG
     HVAMVGDGVN DAPALAASNL GVAMGGAGTD TALETADIAL MADDLNKLPF TIRLSQKALS
     IIKQNITFAL GLKALALLLV IPGWLTLWIA IIADMGATLL VTANSLRLMR MKEKVYK
//

If you have problems or comments...

PBIL Back to PBIL home page