BACA1_BACC1
ID BACA1_BACC1 Reviewed; 888 AA.
AC Q73E41;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Calcium-transporting ATPase 1;
DE EC=7.2.2.10;
DE AltName: Full=BACCA1;
GN OrderedLocusNames=BCE_0519;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=23621633; DOI=10.1111/febs.12310;
RA Kotsubei A., Gorgel M., Morth J.P., Nissen P., Andersen J.L.;
RT "Probing determinants of cyclopiazonic acid sensitivity of bacterial Ca2+-
RT ATPases.";
RL FEBS J. 280:5441-5449(2013).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000269|PubMed:23621633}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000269|PubMed:23621633};
CC -!- ACTIVITY REGULATION: Inhibited by cyclopiazonic acid (CPA).
CC {ECO:0000269|PubMed:23621633}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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DR EMBL; AE017194; AAS39454.1; -; Genomic_DNA.
DR RefSeq; WP_000073702.1; NC_003909.8.
DR AlphaFoldDB; Q73E41; -.
DR SMR; Q73E41; -.
DR EnsemblBacteria; AAS39454; AAS39454; BCE_0519.
DR GeneID; 59159133; -.
DR KEGG; bca:BCE_0519; -.
DR HOGENOM; CLU_002360_2_1_9; -.
DR OMA; GVHRMAK; -.
DR Proteomes; UP000002527; Chromosome.
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-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Calcium transport; Cell membrane; Ion transport;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..888
FT /note="Calcium-transporting ATPase 1"
FT /id="PRO_0000424525"
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 865..885
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 331
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 710
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 714
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 888 AA; 97851 MW; C2AA75EC23AF51B2 CRC64;
MSNWYSKTKD QTLIDLETNE QHGLTEEIAS ERLKQYGSNE LATKQKRTLW QRIFAQINDV
LVYVLIIAAL ISAFVGEWAD ASIIALVVVL NAVIGVVQES KAEQALEALK KMATPKAIVK
RDGELKEIPS EHVVPGDIVM LDAGRYIPCD LRLIETANLK VEESALTGES VPVDKDAIYH
PSMQSDEQVP LGDQKNMAFM STLVTYGRGV GVAVETGMNS QIGKIATLLH EADDDMTPLQ
KSLAQVGKYL GFVAVAICIV MFLIGFLQRR DTLEMFMTAI SLAVAAIPEG LPAIVSIVLA
IGVQRMIKQN VIIRKLPAVE ALGSVTIICS DKTGTLTQNK MTVTHFYSDN TYDQLENLNV
NNDVQRLLLE NMVLCNDASY NNESQTGDPT EIALLVAGST FNMQKDYLEK IHERINELPF
DSDRKMMSTV HTYDESYYSM TKGAIDKLLP RCTHILKNGK IEVLTEADKN QILEAARAMS
REALRVLSFA FKQYNSSNVD IDHLEENLIF IGLVGMIDPP RTEVKDSITE CKKAGIRTVM
ITGDHKDTAF AIAKELGIAE DICEIMIGTE LDNISDTELA SKIDHLHVFA RVSPEHKVKI
VKALRAKGNI VSMTGDGVND APSLKQADVG VAMGITGTDV AKGAADVVLT DDNFSSIVKA
VEEGRNIYRN IKKSILFLLS CNFGEIITLF LAILLGWATP LRPIHILWVN LITDTLPALS
LGVDPEDPDV MKEKPRHAKE SLFSGSVPFL IFNGVVIGLL TLIAFIAGAK FYTGDTNLFP
LFPERIDEDA LLHAQTMAFV VLSFSQLVHS FNLRSRTKSI FSIGIFTNKY LVFSLLIGVL
MQVCIISIPP LANIFGVHAL TLRDWGFVLL LSIIPLVVNE IIKLAKKN
