ATCL_BACSU
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 03-AUG-2022, entry version 152.
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; Firmicutes; 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, DEVELOPMENTAL STAGE, AND DISRUPTION
RP 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; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expressed from 4 hours and peaks at 9 hours after
CC onset of sporulation. {ECO:0000269|PubMed:12161109}.
CC -!- DISRUPTION PHENOTYPE: Spores are less resistant to heat and germinate
CC at a slower rate. {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}.
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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; O34431; -.
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 OMA; PLWNNMM; -.
DR PhylomeDB; O34431; -.
DR BioCyc; BSUB:BSU15650-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:ion transmembrane transport; IBA:GO_Central.
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; IPR005782; P-type_ATPase_IIA.
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 PRINTS; PR00120; HATPASE.
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; TIGR01116; ATPase-IIA1_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
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:0000250"
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
