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Calcium-transporting ATPase (EC 3.6.3.8) (Ca(2 )-ATPase) (Calcium pump) (Calcium-dependent ATPase)

 CDA_MYROD               Reviewed;         548 AA.
Q47910;
19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
19-MAR-2014, sequence version 2.
28-FEB-2018, entry version 66.
RecName: Full=Calcium-transporting ATPase {ECO:0000303|PubMed:1386366};
EC=3.6.3.8 {ECO:0000269|PubMed:1386366};
AltName: Full=Ca(2+)-ATPase {ECO:0000303|PubMed:1386366, ECO:0000303|PubMed:8617788, ECO:0000303|PubMed:8632017, ECO:0000312|EMBL:AAC41526.1};
AltName: Full=Calcium pump {ECO:0000303|PubMed:1386366, ECO:0000303|PubMed:8632017};
AltName: Full=Calcium-dependent ATPase {ECO:0000303|PubMed:8617788};
Flags: Precursor;
Name=cda {ECO:0000303|PubMed:8617788};
Myroides odoratus (Flavobacterium odoratum).
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
Flavobacteriaceae; Myroides.
NCBI_TaxID=256;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC41526.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, ENZYME
REGULATION, SUBCELLULAR LOCATION, AND MOTIF.
STRAIN=ATCC 29979 / NCTC 11179 {ECO:0000312|EMBL:AAC41526.1};
PubMed=8617788; DOI=10.1074/jbc.271.9.5095;
Peiffer W.E., Desrosiers M.G., Menick D.R.;
"Cloning and expression of the unique Ca2+-ATPase from Flavobacterium
odoratum.";
J. Biol. Chem. 271:5095-5100(1996).
[2] {ECO:0000305}
PROTEIN SEQUENCE OF 22-43, FUNCTION, COFACTOR, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 29979 / NCTC 11179 {ECO:0000269|PubMed:8632017};
PubMed=8632017; DOI=10.1074/jbc.271.7.3945;
Desrosiers M.G., Gately L.J., Gambel A.M., Menick D.R.;
"Purification and characterization of the Ca2+-ATPase of
Flavobacterium odoratum.";
J. Biol. Chem. 271:3945-3951(1996).
[3] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, AND
SUBCELLULAR LOCATION.
STRAIN=ATCC 29979 / NCTC 11179 {ECO:0000269|PubMed:1386366}, and
ATCC 4651 / DSM 2801 / JCM 7458 / NBRC 14945 / NCTC 11036
{ECO:0000269|PubMed:1386366};
PubMed=1386366;
Gambel A.M., Desrosiers M.G., Menick D.R.;
"Characterization of a P-type Ca(2+)-ATPase from Flavobacterium
odoratum.";
J. Biol. Chem. 267:15923-15931(1992).
-!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the
transport of calcium. Has some hydrolysis activity also with dATP,
GTP, UTP, ITP and 4-nitrophenyl phosphate as substrate. No
activity with ADP, CTP, acetyl dihydrogen phosphate or AMP-PNP as
substrate. {ECO:0000269|PubMed:1386366,
ECO:0000269|PubMed:8617788, ECO:0000269|PubMed:8632017}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate
+ Ca(2+)(Side 2). {ECO:0000269|PubMed:1386366}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:1386366,
ECO:0000269|PubMed:8617788, ECO:0000269|PubMed:8632017};
-!- ENZYME REGULATION: Completely inhibited by vanadate(3-). Also
inhibited by lanthanoid atom and phosphate. Not inhibited by N-
ethylmaleimide, 1,3-dicyclohexylcarbodiimide, oligomycin, ouabain,
valinomycin, nigericin, thapsigargin, cyclopiazonic acid or
fluorescein isothiocyanate. {ECO:0000269|PubMed:1386366,
ECO:0000269|PubMed:8617788, ECO:0000269|PubMed:8632017}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.5 uM for calcium (at 8 degrees Celsius)
{ECO:0000269|PubMed:8632017};
KM=90 uM for ATP (at 8 degrees Celsius)
{ECO:0000269|PubMed:8632017};
Vmax=75 umol/min/mg enzyme toward ATP (at 8 degrees Celsius)
{ECO:0000269|PubMed:8632017};
pH dependence:
Optimum pH is 8.0 for ATP hydrolysis activity. Loses 50% of the
activity at pH 7.0 or 8.5, has less than 20% activity at pH 6.5
and virtually no activity at pH 9.0.
{ECO:0000269|PubMed:8632017};
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:1386366, ECO:0000269|PubMed:8617788,
ECO:0000269|PubMed:8632017}; Peripheral membrane protein
{ECO:0000269|PubMed:1386366, ECO:0000269|PubMed:8617788,
ECO:0000269|PubMed:8632017}; Periplasmic side
{ECO:0000269|PubMed:1386366, ECO:0000269|PubMed:8617788,
ECO:0000269|PubMed:8632017}.
-!- SEQUENCE CAUTION:
Sequence=AAC41526.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; L42816; AAC41526.1; ALT_INIT; Genomic_DNA.
SMR; Q47910; -.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0004035; F:alkaline phosphatase activity; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042623; F:ATPase activity, coupled; IDA:UniProtKB.
GO; GO:0005388; F:calcium-transporting ATPase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0071286; P:cellular response to magnesium ion; IDA:UniProtKB.
CDD; cd16016; AP-SPAP; 1.
Gene3D; 3.40.720.10; -; 2.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR026263; Alkaline_phosphatase_prok.
InterPro; IPR002591; Phosphodiest/P_Trfase.
Pfam; PF01663; Phosphodiest; 1.
PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
SUPFAM; SSF53649; SSF53649; 2.
1: Evidence at protein level;
ATP-binding; Calcium; Calcium transport; Cell inner membrane;
Cell membrane; Direct protein sequencing; Hydrolase; Ion transport;
Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Signal; Transport.
SIGNAL 1 21 {ECO:0000269|PubMed:8632017}.
CHAIN 22 548 Calcium-transporting ATPase.
{ECO:0000269|PubMed:8632017}.
/FTId=PRO_0000425600.
REGION 160 162 Substrate binding.
{ECO:0000250|UniProtKB:A1YYW7}.
MOTIF 179 187 ATP-binding. {ECO:0000255,
ECO:0000303|PubMed:8617788}.
ACT_SITE 78 78 Phosphothreonine intermediate.
{ECO:0000250|UniProtKB:A1YYW7}.
METAL 37 37 Divalent metal cation 1.
{ECO:0000250|UniProtKB:A1YYW7}.
METAL 78 78 Divalent metal cation 1.
{ECO:0000250|UniProtKB:A1YYW7}.
METAL 305 305 Divalent metal cation 2.
{ECO:0000250|UniProtKB:A1YYW7}.
METAL 309 309 Divalent metal cation 2; via tele
nitrogen. {ECO:0000250|UniProtKB:A1YYW7}.
METAL 352 352 Divalent metal cation 1.
{ECO:0000250|UniProtKB:A1YYW7}.
METAL 353 353 Divalent metal cation 1; via tele
nitrogen. {ECO:0000250|UniProtKB:A1YYW7}.
METAL 488 488 Divalent metal cation 2; via tele
nitrogen. {ECO:0000250|UniProtKB:A1YYW7}.
BINDING 99 99 Substrate.
{ECO:0000250|UniProtKB:A1YYW7}.
SEQUENCE 548 AA; 61156 MW; 644DB1EDE497F7FD CRC64;
MNFKSTVITA MCCFFSFAVL ASEKLEKPKL VVGLVVDQMR WDYLYRYYDR YSENGFKRLL
NEGFSSENTL IDYVPTYTAI GHSTIYTGSV PAINGIAGND FIIQATGQNM YCTQDDSVQA
VGGEGKVGQQ SPKNLLVSTI TDQLKLATNF QSKVIGIAIK DRGGILPAGH FANAAYWLDG
KTGDWITSTY YMKDLPKWVK GFNKEKVVDQ YYKQGWKTLY PIDTYVLSTA DDNLYEETFK
GEKTPTFPRD LVKLKKENGY ELIKSTPQGN TLTLDFAKRA IENEQLGNNP LQVTDFLAVS
LSSTDYIGHQ FAINSIEIED TYLRLDRDIA DFLAYLDQNI GKGNYTLFLS ADHGAAHNPK
FFADQKGNSG YFDTKAIRKD LNEKLASKFG VADLVKSLAN YQVHLNYEVI EANDVEEDEV
IAAAIKLLKK VDGVAFVVDM NEAAESSVPQ ILRERIINGY NFKRSGAIQL ILEPQWFSGS
KDGKGTTHGS WNSYDAHIPA VFLGWGVKPG KTTRQTHMTD IAPTIAQILK IEFPNGNIGT
PIQEAIEQ


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