ID A0A0H3J990_CLOPA Unreviewed; 876 AA.
AC A0A0H3J990;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 28-JAN-2026, entry version 48.
DE RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
GN ORFNames=CLPA_c16100 {ECO:0000313|EMBL:AJA51673.1}, CP6013_01567
GN {ECO:0000313|EMBL:KRU12320.1};
OS Clostridium pasteurianum DSM 525 = ATCC 6013.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA51673.1, ECO:0000313|Proteomes:UP000030905};
RN [1] {ECO:0000313|EMBL:AJA51673.1, ECO:0000313|Proteomes:UP000030905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 525 {ECO:0000313|EMBL:AJA51673.1}, and DSM 525 / ATCC 6013
RC {ECO:0000313|Proteomes:UP000030905};
RX PubMed=25700415;
RA Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.;
RT "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing
RT Clostridium pasteurianum DSM 525.";
RL Genome Announc. 3:e01591-e01514(2015).
RN [2] {ECO:0000313|EMBL:KRU12320.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU12320.1};
RA Pyne M.E., Utturkar S.M., Brown S.D., Moo-Young M., Chung D.A., Chou P.C.;
RT "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT 6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KRU12320.1, ECO:0000313|Proteomes:UP000028042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU12320.1,
RC ECO:0000313|Proteomes:UP000028042};
RX PubMed=25103768;
RA Pyne M.E., Utturkar S., Brown S.D., Moo-Young M., Chung D.A., Chou C.P.;
RT "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT 6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL Genome Announc. 2:0-0(0).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
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:0000256|ARBA:ARBA00048694};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
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DR EMBL; CP009268; AJA51673.1; -; Genomic_DNA.
DR EMBL; JPGY02000001; KRU12320.1; -; Genomic_DNA.
DR RefSeq; WP_003443456.1; NZ_ANZB01000004.1.
DR AlphaFoldDB; A0A0H3J990; -.
DR GeneID; 93073776; -.
DR KEGG; cpae:CPAST_c16100; -.
DR KEGG; cpat:CLPA_c16100; -.
DR PATRIC; fig|1262449.3.peg.1448; -.
DR eggNOG; COG0474; Bacteria.
DR Proteomes; UP000028042; Unassembled WGS sequence.
DR Proteomes; UP000030905; 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:0140352; P:export from cell; IEA:UniProtKB-ARBA.
DR CDD; cd02089; P-type_ATPase_Ca_prok; 1.
DR FunFam; 2.70.150.10:FF:000016; Calcium-transporting P-type ATPase putative; 1.
DR FunFam; 3.40.50.1000:FF:000028; Calcium-transporting P-type ATPase, putative; 1.
DR FunFam; 3.40.1110.10:FF:000053; Cation-transporting ATPase, E1-E2 family; 1.
DR FunFam; 3.40.50.1000:FF:000001; Phospholipid-transporting ATPase IC; 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; IPR059000; ATPase_P-type_domA.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006413; P-type_ATPase_IIA_PMR1.
DR InterPro; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; 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; SFLDS00003; Haloacid_Dehalogenase; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000313|EMBL:AJA51673.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030905};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 55..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 672..694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 739..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 813..834
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 846..869
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..75
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 876 AA; 95838 MW; B4ED4888593D34CB CRC64;
MWFGKTTEEV IKELKVDPKE GLSSDESKRR LEEYGENKLT SKTQKTLFQI FISQLKDPMI
FILLIAAVIS AFMKELSDSI IILVVILING MVGTIQEFKS EKAMEALKQL STPKAIVKRD
GDLKEIPSEE VVPGDIVILD AGRFTPADLR LIESANLKIE ESALTGESVP SSKDANVNFD
NGNIPLGDQK NMAFASTLAT YGRGIGVVTG TGMNTEIGKI AKMLDESETE MTPLQKKLAE
LSKILGIAAV AICTLIFIIS VIQGRDLFEM FLTAISLAVA AIPEGLPAIV SIVLAMGVQR
MVKNHAIIRK LPAVETLGAV NIICSDKTGT LTQNKMTVKK FYTAGPDELK AVDELDINNI
DDNLLLKNLM LCNDATYTET SQTGDPTEVA LLEMGVKFNI LKADLQTSSP RVNEVPFDSD
RKLMSTINKQ DKNYIVYTKG ATDNLLKIAT KININGNIQD LTEDLKAKII KASNTMSDDA
LRVLGAAYKE LTSPDIPIDS IEKDLIFIGL VGMIDPPRLE VKDSISTCKN SGIKTIMITG
DHRNTAFAIA KELGIAENEN ETISGVELDK LSQEELNNKI DSLRVFARVS PEHKVNIVKA
FKSKGNIVSM TGDGVNDAPS LKIADIGVAM GITGTDVSKG ASDMILTDDN FSTIVSAIKE
GRNIFNNIKK SIIFLLSCNL GEIITLFIAI LLNWDTPLKP IHILWVNLIT DTLPALSLGV
DPGDENVMDN PPRNTKESLF SHGSGIFLIL NGLLIGILTL IAFRYGEKVY GTEGVHAQTM
AFVVLSVSQL FHSLNMRHPR KSIFQVGIFS NKYLVGSIII GILLQYLVIT IPFLSNLFNL
FNLSLFDWTF VILVSVLTLV FNEVAKIFIR AKSKNS
//
