UniProt: K0AYZ7

Database: UniProt
Entry: K0AYZ7_GOTA9

LinkDB:  K0AYZ7_GOTA9 
Original site:  K0AYZ7_GOTA9

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (17)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (25)   

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ID   K0AYZ7_GOTA9            Unreviewed;       903 AA.
AC   K0AYZ7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE            EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
GN   Name=yloB1 {ECO:0000313|EMBL:AFS77900.1};
GN   OrderedLocusNames=Curi_c08270 {ECO:0000313|EMBL:AFS77900.1};
OS   Gottschalkia acidurici (strain ATCC 7906 / DSM 604 / BCRC 14475 / CIP
OS   104303 / KCTC 5404 / NCIMB 10678 / 9a) (Clostridium acidurici).
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Gottschalkiaceae;
OC   Gottschalkia.
OX   NCBI_TaxID=1128398 {ECO:0000313|EMBL:AFS77900.1, ECO:0000313|Proteomes:UP000006094};
RN   [1] {ECO:0000313|EMBL:AFS77900.1, ECO:0000313|Proteomes:UP000006094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7906 / DSM 604 / BCRC 14475 / CIP 104303 / KCTC 5404 /
RC   NCIMB 10678 / 9a {ECO:0000313|Proteomes:UP000006094};
RX   PubMed=23240052; DOI=10.1371/journal.pone.0051662;
RA   Hartwich K., Poehlein A., Daniel R.;
RT   "The purine-utilizing bacterium Clostridium acidurici 9a: a genome-guided
RT   metabolic reconsideration.";
RL   PLoS ONE 7:E51662-E51662(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003326; AFS77900.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0AYZ7; -.
DR   STRING; 1128398.Curi_c08270; -.
DR   KEGG; cad:Curi_c08270; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_3_0_9; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000006094; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
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; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW   Hydrolase {ECO:0000313|EMBL:AFS77900.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022568};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006094};
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:ARBA00022568}.
FT   TRANSMEM        56..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        676..696
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        702..722
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        743..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        777..793
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        814..832
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        852..869
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..76
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   903 AA;  98996 MW;  2DD9FB321083954F CRC64;
     MSWYEKDIEE LSSELNVDIS VGLSEEEVKL RKEKYGENIL KEGKRKSIIS MFFSQFKDFM
     VIILLIASIV SGLLGEISDT VIILLVVLLN ALLGVIQENK AEKSLEALKS LSSPIAKVIR
     NGKRLEVKSS ELVPGDIILL EAGDFVPADG VLFESASLMI EESALTGESV PVEKQINIPE
     GENIPLGDRK NYVFTSSLVT NGRGKVIVTE TGMNTEIGKI AGMLQNQEDM KTPLQEKLDE
     LGKMLGIGAL GICVVIFIIG YLQGTPLLEM FMTSVSLAVA AIPEGLPAIV TVVLSIGVQR
     MISKNAIIRK LPAVETLGTA SVICSDKTGT LTQNKMTVTK LYTYGNLENI EDINISNKDT
     ELALKIGLLC NDSVIETSKE SEGGLGDPTE IALVVSASRH GMDKTNEEKK LERVEEIPFD
     SDRKLMTTVH KDNDGYKVFT KGALDVLLER CKSILIDSEI KDLTEEIKED IRKVNHEMSE
     EALRVIALAY KEESKIPAEM TSEKVENDLI FVGMEGMIDP PREEAKVAVE KCKMAGIKPV
     MITGDHKITA MAIAKELGIL ENQVEAIEGK EIENMSDEDL NKNVEKYSVY ARVSPEHKVR
     IVSAWQNNGK VVAMTGDGVN DAPALKKANI GCAMGITGTD VSKQAADMIL TDDNFATIVS
     AVEEGRSIFD NIKKSIHFLL SCNIGEVVAL FIAVVLGMPI PLLPIHILWV NLVTDSLPAL
     ALGMDPAEPD IMKRKPRDPK KSIFAGGLWT TIIVQGVIIG VITLISFNVG RRTSIELGRT
     MAFITLSLSQ IVHTLNVRSI DKSIFKMGLF SNKYLVGADL LSILSVSIII IIPKLREVFK
     LTTISGTQLL DIIGLTLTPL IVVEIVKLFK RKIKNRNYFS SLTYKFIESQ RQAITDKESE
     GTK
//

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