CDA_MYROD
ID CDA_MYROD Reviewed; 548 AA.
AC Q47910;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000303|PubMed:1386366};
DE EC=7.2.2.10 {ECO:0000269|PubMed:1386366};
DE AltName: Full=Ca(2+)-ATPase {ECO:0000303|PubMed:1386366, ECO:0000303|PubMed:8617788, ECO:0000303|PubMed:8632017, ECO:0000312|EMBL:AAC41526.1};
DE AltName: Full=Calcium pump {ECO:0000303|PubMed:1386366, ECO:0000303|PubMed:8632017};
DE AltName: Full=Calcium-dependent ATPase {ECO:0000303|PubMed:8617788};
DE Flags: Precursor;
GN Name=cda {ECO:0000303|PubMed:8617788};
OS Myroides odoratus (Flavobacterium odoratum).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Myroides.
OX NCBI_TaxID=256;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC41526.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND MOTIF.
RC STRAIN=ATCC 29979 / DSM 2802 / NCTC 11179 / CL41/66
RC {ECO:0000312|EMBL:AAC41526.1};
RX PubMed=8617788; DOI=10.1074/jbc.271.9.5095;
RA Peiffer W.E., Desrosiers M.G., Menick D.R.;
RT "Cloning and expression of the unique Ca2+-ATPase from Flavobacterium
RT odoratum.";
RL J. Biol. Chem. 271:5095-5100(1996).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 22-43, FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29979 / DSM 2802 / NCTC 11179 / CL41/66
RC {ECO:0000269|PubMed:8632017};
RX PubMed=8632017; DOI=10.1074/jbc.271.7.3945;
RA Desrosiers M.G., Gately L.J., Gambel A.M., Menick D.R.;
RT "Purification and characterization of the Ca2+-ATPase of Flavobacterium
RT odoratum.";
RL J. Biol. Chem. 271:3945-3951(1996).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29979 / DSM 2802 / NCTC 11179 / CL41/66
RC {ECO:0000269|PubMed:1386366}, and
RC ATCC 4651 / DSM 2801 / BCRC 10678 / JCM 7458 / NBRC 14945 / NCTC 11036
RC {ECO:0000269|PubMed:1386366};
RX PubMed=1386366; DOI=10.1016/s0021-9258(19)49622-1;
RA Gambel A.M., Desrosiers M.G., Menick D.R.;
RT "Characterization of a P-type Ca(2+)-ATPase from Flavobacterium odoratum.";
RL J. Biol. Chem. 267:15923-15931(1992).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. Has some hydrolysis activity also with dATP, GTP, UTP, ITP and
CC 4-nitrophenyl phosphate as substrate. No activity with ADP, CTP, acetyl
CC dihydrogen phosphate or AMP-PNP as substrate.
CC {ECO:0000269|PubMed:1386366, ECO:0000269|PubMed:8617788,
CC ECO:0000269|PubMed:8632017}.
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:1386366};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1386366, ECO:0000269|PubMed:8617788,
CC ECO:0000269|PubMed:8632017};
CC -!- ACTIVITY REGULATION: Completely inhibited by vanadate(3-). Also
CC inhibited by lanthanoid atom and phosphate. Not inhibited by N-
CC ethylmaleimide, 1,3-dicyclohexylcarbodiimide, oligomycin, ouabain,
CC valinomycin, nigericin, thapsigargin, cyclopiazonic acid or fluorescein
CC isothiocyanate. {ECO:0000269|PubMed:1386366,
CC ECO:0000269|PubMed:8617788, ECO:0000269|PubMed:8632017}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for calcium (at 8 degrees Celsius)
CC {ECO:0000269|PubMed:8632017};
CC KM=90 uM for ATP (at 8 degrees Celsius) {ECO:0000269|PubMed:8632017};
CC Vmax=75 umol/min/mg enzyme toward ATP (at 8 degrees Celsius)
CC {ECO:0000269|PubMed:8632017};
CC pH dependence:
CC Optimum pH is 8.0 for ATP hydrolysis activity. Loses 50% of the
CC activity at pH 7.0 or 8.5, has less than 20% activity at pH 6.5 and
CC virtually no activity at pH 9.0. {ECO:0000269|PubMed:8632017};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:1386366,
CC ECO:0000269|PubMed:8617788, ECO:0000269|PubMed:8632017}; Peripheral
CC membrane protein {ECO:0000269|PubMed:1386366,
CC ECO:0000269|PubMed:8617788, ECO:0000269|PubMed:8632017}; Periplasmic
CC side {ECO:0000269|PubMed:1386366, ECO:0000269|PubMed:8617788,
CC ECO:0000269|PubMed:8632017}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC41526.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L42816; AAC41526.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q47910; -.
DR SMR; Q47910; -.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0005388; F:P-type calcium transporter activity; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0071286; P:cellular response to magnesium ion; IDA:UniProtKB.
DR CDD; cd16016; AP-SPAP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR026263; Alkaline_phosphatase_prok.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR Pfam; PF01663; Phosphodiest; 1.
DR PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Calcium transport; Cell inner membrane;
KW Cell membrane; Direct protein sequencing; Ion transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Signal;
KW Translocase; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:8632017"
FT CHAIN 22..548
FT /note="Calcium-transporting ATPase"
FT /evidence="ECO:0000269|PubMed:8632017"
FT /id="PRO_0000425600"
FT MOTIF 179..187
FT /note="ATP-binding"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:8617788"
FT ACT_SITE 78
FT /note="Phosphothreonine intermediate"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 37
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 78
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 160..162
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 305
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 309
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 352
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 353
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 488
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
SQ 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
