ID A0A3D9DI54_9FLAO Unreviewed; 679 AA. AC A0A3D9DI54; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 10-FEB-2021, entry version 10. DE RecName: Full=Potassium-transporting ATPase ATP-binding subunit {ECO:0000256|HAMAP-Rule:MF_00285}; DE EC=7.2.2.6 {ECO:0000256|HAMAP-Rule:MF_00285}; DE AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain {ECO:0000256|HAMAP-Rule:MF_00285}; DE AltName: Full=Potassium-binding and translocating subunit B {ECO:0000256|HAMAP-Rule:MF_00285}; DE AltName: Full=Potassium-translocating ATPase B chain {ECO:0000256|HAMAP-Rule:MF_00285}; GN Name=kdpB {ECO:0000256|HAMAP-Rule:MF_00285, GN ECO:0000313|EMBL:REC77521.1}; GN ORFNames=DRF60_11075 {ECO:0000313|EMBL:REC77521.1}; OS Chryseobacterium elymi. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae; OC Chryseobacterium group; Chryseobacterium. OX NCBI_TaxID=395936 {ECO:0000313|EMBL:REC77521.1, ECO:0000313|Proteomes:UP000257030}; RN [1] {ECO:0000313|EMBL:REC77521.1, ECO:0000313|Proteomes:UP000257030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 22547 {ECO:0000313|EMBL:REC77521.1, RC ECO:0000313|Proteomes:UP000257030}; RX PubMed=20185262; DOI=10.1016/j.syapm.2009.12.004; RA Cho S.H., Lee K.S., Shin D.S., Han J.H., Park K.S., Lee C.H., Park K.H., RA Kim S.B.; RT "Four new species of Chryseobacterium from the rhizosphere of coastal sand RT dune plants, Chryseobacterium elymi sp. nov., Chryseobacterium hagamense RT sp. nov., Chryseobacterium lathyri sp. nov. and Chryseobacterium RT rhizosphaerae sp. nov."; RL Syst. Appl. Microbiol. 33:122-127(2010). 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. CC {ECO:0000256|HAMAP-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:0000256|HAMAP- CC Rule:MF_00285}; CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB CC and KdpC. {ECO:0000256|HAMAP-Rule:MF_00285}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00285}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00285}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type IA subfamily. {ECO:0000256|HAMAP-Rule:MF_00285}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:REC77521.1}. 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; QNUH01000008; REC77521.1; -; Genomic_DNA. DR Proteomes; UP000257030; Unassembled WGS sequence. 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008556; F:potassium transmembrane transporter activity, phosphorylative mechanism; 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 PANTHER; PTHR43743; PTHR43743; 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 {ECO:0000256|HAMAP-Rule:MF_00285}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00285}; Hydrolase {ECO:0000313|EMBL:REC77521.1}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_00285}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00285}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00285}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00285}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00285}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP- KW Rule:MF_00285}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00285}; KW Potassium transport {ECO:0000256|ARBA:ARBA00022538, ECO:0000256|HAMAP- KW Rule:MF_00285}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_00285}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00285}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00285}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00285}. FT TRANSMEM 35..56 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 62..83 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 222..242 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 254..277 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 583..602 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 614..635 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 655..678 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT NP_BIND 376..383 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT ACT_SITE 310 FT /note="4-aspartylphosphate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT METAL 517 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT METAL 521 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT BINDING 347 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT BINDING 351 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT BINDING 394 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" SQ SEQUENCE 679 AA; 73396 MW; 1612C977E1FDC039 CRC64; MKNQSQTLFQ KDLVNEAIKQ SFVKLNPKIM FKNPVMFLVE VGTVVMFIVS LFSLTGDKSQ GSFAYNFTVF IILFFTVLFA NFAEAIAEAR GKAQADTLRK TREETPAKVV VDNKPGFQVE TVLRMSAEMK LGDIFLCETG DQIPMDGEII EGLATIDESA ITGESAPVIR ESGGDKSSVT GGTKVLSDRI KVKVTTKPGE SFLDKMIALV EGASRQKTPN EIALTILLAG FTLTFIIVTL TLKPFADYAQ TPITIAAFIS LFVCLIPTTI GGLLSAIGIA GMDRALRANV ITKSGKAVET AGDIDVLLLD KTGTITIGNR KATEFHPADG IGMPDFIKAS ALSSVADETP EGKSIIELSQ LKSEDLLVPN PVYIDFSAET RTSGIDFENT RIRKGAYDTI KKLTEKAGNI FPEETQNAIT KISENGGTPL VVSVNEKVWG VIELQDIIKT GIQERFQRLR KMGVKTVMVT GDNPLTAKFI AEKAGVDDFI AEAKPEDKMN YIKKEQQEGK LVAMMGDGTN DAPALAQADV GVAMNSGTQA AKEAGNMVDL DNDPTKLIEI VEIGKQLLMT RGTLTTFSIA NDVAKYFAII PALFITFIPS LQKLNIMNLH SPETAILSAV IFNAVIIPFL IPLALKGVAY KPIGASALLR RNLLIYGLGG VIVPFIGIKI IDLVISLFY //