KDPB_CLOP1
ID KDPB_CLOP1 Reviewed; 688 AA.
AC Q0TRT3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Potassium-transporting ATPase ATP-binding subunit {ECO:0000255|HAMAP-Rule:MF_00285};
DE EC=7.2.2.6 {ECO:0000255|HAMAP-Rule:MF_00285};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain {ECO:0000255|HAMAP-Rule:MF_00285};
DE AltName: Full=Potassium-binding and translocating subunit B {ECO:0000255|HAMAP-Rule:MF_00285};
DE AltName: Full=Potassium-translocating ATPase B chain {ECO:0000255|HAMAP-Rule:MF_00285};
GN Name=kdpB {ECO:0000255|HAMAP-Rule:MF_00285}; OrderedLocusNames=CPF_1211;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
CC -!- FUNCTION: Part of the high-affinity ATP-driven potassium transport (or
CC Kdp) system, which catalyzes the hydrolysis of ATP coupled with the
CC electrogenic transport of potassium into the cytoplasm. This subunit is
CC responsible for energy coupling to the transport system and for the
CC release of the potassium ions to the cytoplasm. {ECO:0000255|HAMAP-
CC Rule:MF_00285}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + phosphate;
CC Xref=Rhea:RHEA:16777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16778;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00285};
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC. {ECO:0000255|HAMAP-Rule:MF_00285}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00285};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00285}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IA subfamily. {ECO:0000255|HAMAP-Rule:MF_00285}.
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; CP000246; ABG84790.1; -; Genomic_DNA.
DR RefSeq; WP_003456252.1; NC_008261.1.
DR AlphaFoldDB; Q0TRT3; -.
DR SMR; Q0TRT3; -.
DR STRING; 195103.CPF_1211; -.
DR EnsemblBacteria; ABG84790; ABG84790; CPF_1211.
DR GeneID; 29571673; -.
DR KEGG; cpf:CPF_1211; -.
DR eggNOG; COG2216; Bacteria.
DR HOGENOM; CLU_025728_2_0_9; -.
DR OMA; KSPVMFV; -.
DR OrthoDB; 237367at2; -.
DR Proteomes; UP000001823; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR CDD; cd02078; P-type_ATPase_K; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_00285; KdpB; 1.
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; IPR006391; P-type_ATPase_bsu_IA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR43743; PTHR43743; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR01497; kdpB; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW Potassium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..688
FT /note="Potassium-transporting ATPase ATP-binding subunit"
FT /id="PRO_1000022436"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT ACT_SITE 313
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 383..390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 524
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 528
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
SQ SEQUENCE 688 AA; 73833 MW; 4414BCC4B94659E8 CRC64;
MKEKENSLFN SKMIKRAMKD SFIKLNPKIQ LQNPVMFIVY IASILTTVLY VFSLFGIKDN
SPSFILFISI LLWFTVLFAN FAEAIAEGRG KAQADALRSA KKDILANRIE SIETKEKVSK
VNSTELRKGD LIIVKAGEQI PADGDVVYGA ASVDESAITG ESAPVIRESG GDRSAVTGGT
QVISDYIVVK VSNNPGESFM DKMIAMVEGA SRKKTPNEIA LQILLVSLTI IFLVVTASLY
AYSEFASNQN GVINSTSVTS LLALLVCLAP TTIGALLSAI GIAGMSRLNQ ANVLAMSGRA
IEAAGDVDIL MLDKTGTITL GNRQASEFLP VDGANIEELA DAAQLSSLAD ETPEGRSIVI
LAKEQFGIRG RDLSSSNAKF IEFTAKTRMS GVDFNGDEIR KGSAESIKKY ITEHGGDFSD
ECEKKVEEIA RKGGTPLVVA KNYKVLGIIY LKDIVKRGVK EKFSDLRKMG IKTIMITGDN
PLTAAAIAAE AGVDDFLAEA TPEGKLNMIK DFQKKGHLVA MTGDGTNDAP ALAQADVAVA
MNTGTQAAKE AGNMVDLDSS PTKLIEIVKI GKQLLMTRGA LTTFSIANDI AKYFAIIPPL
FIGLFPELSR LNIMNLQSPE SAILSAVIYN AFIIIFLIPL ALKGVKYREV SANKLLSRNL
FVYGLGGIIA PFIAIKGIDI LITMLGIV
