KDPB_CLOAB
ID KDPB_CLOAB Reviewed; 685 AA.
AC O32328;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 154.
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=CA_C3681;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=9226259; DOI=10.1128/jb.179.14.4501-4512.1997;
RA Treuner-Lange A., Kuhn A., Duerre P.;
RT "The kdp system of Clostridium acetobutylicum: cloning, sequencing, and
RT transcriptional regulation in response to potassium concentration.";
RL J. Bacteriol. 179:4501-4512(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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, ECO:0000269|PubMed:9226259}.
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 ECO:0000269|PubMed:9226259}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:9226259}.
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}.
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DR EMBL; U44892; AAC45478.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK81602.1; -; Genomic_DNA.
DR PIR; G97351; G97351.
DR PIR; T46843; T46843.
DR RefSeq; NP_350262.1; NC_003030.1.
DR RefSeq; WP_010966942.1; NC_003030.1.
DR AlphaFoldDB; O32328; -.
DR SMR; O32328; -.
DR STRING; 272562.CA_C3681; -.
DR EnsemblBacteria; AAK81602; AAK81602; CA_C3681.
DR GeneID; 45000179; -.
DR KEGG; cac:CA_C3681; -.
DR PATRIC; fig|272562.8.peg.3870; -.
DR eggNOG; COG2216; Bacteria.
DR HOGENOM; CLU_025728_2_0_9; -.
DR OMA; ILWLWFT; -.
DR OrthoDB; 237367at2; -.
DR Proteomes; UP000000814; 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; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..685
FT /note="Potassium-transporting ATPase ATP-binding subunit"
FT /id="PRO_0000046113"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT ACT_SITE 306
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 375..382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 517
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT CONFLICT 25..26
FT /note="LN -> IK (in Ref. 1; AAC45478)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="A -> R (in Ref. 1; AAC45478)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="G -> A (in Ref. 1; AAC45478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 685 AA; 73686 MW; FD57B24E938F4402 CRC64;
MKSKKSKFIT KDILKEAIIE SFKKLNPKYM MKNPVMFVVE VGFFVTILLT IFPSIFGDKG
HNLRVYNLIV TIILFITVLF ANFAESVAEG RGKAQADALK KTRKDTIAKL IGKDGSIKTI
NANELKKGDV VLVENGDVIP NDGEVVDGVA SVDESAITGE SAPVMKEPGG DFASVTGGTK
VVSDWLKVEI TATPGESFLD KMINLVEGAS RQKTPNEIAL NTILVSLTLI FLIVLVALYP
MATYTGVKIP MSTLIALLVC LIPTTIGGLL SAIGIAGMDR VTRFNVIAMS GKAVEACGDV
DTMILDKTGT ITYGNRLAAD FITVGGADKQ KLIDYSVMCS LKDDTPEGKS IVELGKQLGI
TIDTKKYESI EFEEFTAQTR MSGIKLENGT AVKKGAYDAI KKRVQELKGV IPKDLDEAVN
KVAKLGGTPL VVCVDNKIYG VIYLKDTVKP GLVERFERLR EIGIKTIMCT GDNPLTAATI
AKEAGVDGFI AECKPEDKIE AIKKEQDEGK LVAMTGDGTN DAPALAQADV GLAMNSGTTA
AKEAANMVDL DSDPTKVLEV VEIGKQLLIT RGALTTFSIA NDVAKYFAII PAIFTIAIPK
MQLMNIMHLS TPYSAILSAL IFNAIIIPAL IPIAMKGVKY RPMKSEALLL RNMIVFGFGG
IIVPFVGIKI IDMIITPMVR ILNLG
