ID   ATCL_BACSU              Reviewed;         890 AA.
AC   O34431; Q799L2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Calcium-transporting ATPase;
DE            EC=7.2.2.10;
DE   AltName: Full=Calcium pump;
GN   Name=yloB; OrderedLocusNames=BSU15650;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA   Foulger D., Errington J.;
RT   "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT   genome.";
RL   Microbiology 144:801-805(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP   INDUCTION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PS832;
RX   PubMed=12161109; DOI=10.1016/s0143-4160(02)00125-2;
RA   Raeymaekers L., Wuytack E., Willems I., Michiels C.W., Wuytack F.;
RT   "Expression of a P-type Ca(2+)-transport ATPase in Bacillus subtilis during
RT   sporulation.";
RL   Cell Calcium 32:93-93(2002).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the transport of calcium.
CC       {ECO:0000269|PubMed:12161109}.
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:12161109};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12161109};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from 4 hours and peaks at 9 hours after
CC       onset of sporulation. {ECO:0000269|PubMed:12161109}.
CC   -!- INDUCTION: Expressed under control of sigma-F (sigF).
CC       {ECO:0000269|PubMed:12161109}.
CC   -!- PTM: Phosphorylated in a Ca(2+)-dependent manner starting 4 hours after
CC       shifting to sporulation medium. {ECO:0000269|PubMed:12161109}.
CC   -!- DISRUPTION PHENOTYPE: Spores are less resistant to heat and germinate
CC       at a slower rate, Ca(2+)-dependent phosphorylation is no longer seen.
CC       {ECO:0000269|PubMed:12161109}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIA subfamily. {ECO:0000305}.
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; Y13937; CAA74269.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13439.1; -; Genomic_DNA.
DR   PIR; H69877; H69877.
DR   RefSeq; NP_389448.1; NC_000964.3.
DR   RefSeq; WP_003232087.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34431; -.
DR   SMR; O34431; -.
DR   IntAct; O34431; 1.
DR   STRING; 224308.BSU15650; -.
DR   PaxDb; 224308-BSU15650; -.
DR   EnsemblBacteria; CAB13439; CAB13439; BSU_15650.
DR   GeneID; 936954; -.
DR   KEGG; bsu:BSU15650; -.
DR   PATRIC; fig|224308.179.peg.1705; -.
DR   eggNOG; COG0474; Bacteria.
DR   InParanoid; O34431; -.
DR   OrthoDB; 9813266at2; -.
DR   PhylomeDB; O34431; -.
DR   BioCyc; BSUB:BSU15650-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
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   GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IBA:GO_Central.
DR   CDD; cd02089; P-type_ATPase_Ca_prok; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR005782; P-type_ATPase_IIA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Calcium transport; Cell membrane; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..890
FT                   /note="Calcium-transporting ATPase"
FT                   /id="PRO_0000360851"
FT   TOPO_DOM        1..47
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        48..68
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        69..78
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        79..99
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        100..238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        239..258
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        259..270
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        271..288
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        289..688
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        689..708
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        709..718
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        719..739
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        740..759
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        760..782
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        783..798
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        799..818
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        819..830
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        831..849
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        850..864
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        865..885
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        886..890
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        326
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000305|PubMed:12161109"
FT   BINDING         279
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         633
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         637
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         699
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         702
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         727
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         730
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         731
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         731
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   890 AA;  97293 MW;  43CB25F7A9BA31A6 CRC64;
     MKFHEMGQTD LLEATNTSMK QGLTEKEVKK RLDKHGPNEL QEGKKTSALL LFFAQFKDFM
     VLVLLAATLI SGFLGEYVDA VAIIAIVFVN GILGFFQERR AEQSLQALKE LSTPHVMALR
     EGSWTKIPSK ELVPGDIVKF TSGDRIGADV RIVEARSLEI EESALTGESI PVVKHADKLK
     KPDVSLGDIT NMAFMGTIVT RGSGVGVVVG TGMNTAMGKI ADMLESAGTL STPLQRRLEQ
     LGKILIVVAL LLTVLVVAVG VIQGHDLYSM FLAGVSLAVA AIPEGLPAIV TVALSLGVQR
     MIKQKSIVRK LPAVETLGCA SIICSDKTGT MTQNKMTVTH VWSGGKTWRV AGAGYEPKGS
     FTLNEKEISV NEHKPLQQML LFGALCNNSN IEKRDGEYVL DGDPTEGALL TAARKGGFSK
     EFVESNYRVI EEFPFDSARK MMTVIVENQD RKRYIITKGA PDVLMQRSSR IYYDGSAALF
     SNERKAETEA VLRHLASQAL RTIAVAYRPI KAGETPSMEQ AEKDLTMLGL SGIIDPPRPE
     VRQAIKECRE AGIKTVMITG DHVETAKAIA KDLRLLPKSG KIMDGKMLNE LSQEELSHVV
     EDVYVFARVS PEHKLKIVKA YQENGHIVAM TGDGVNDAPA IKQADIGVSM GITGTDVAKE
     ASSLVLVDDN FATIKSAIKE GRNIYENIRK FIRYLLASNV GEILVMLFAM LLALPLPLVP
     IQILWVNLVT DGLPAMALGM DQPEGDVMKR KPRHPKEGVF ARKLGWKVVS RGFLIGVATI
     LAFIIVYHRN PENLAYAQTI AFATLVLAQL IHVFDCRSET SVFSRNPFQN LYLIGAVLSS
     ILLMLVVIYY PPLQPIFHTV AITPGDWMLV IGMSAIPTFL LAGSLLTRKK
//