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-APR-2019, entry version 3. 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; OC Flavobacteriaceae; 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., RA Park K.H., Kim S.B.; RT "Four new species of Chryseobacterium from the rhizosphere of coastal RT sand dune plants, Chryseobacterium elymi sp. nov., Chryseobacterium RT hagamense sp. nov., Chryseobacterium lathyri sp. nov. and RT Chryseobacterium rhizosphaerae sp. nov."; RL Syst. Appl. Microbiol. 33:122-127(2010). CC -!- FUNCTION: Part of the high-affinity ATP-driven potassium transport CC (or Kdp) system, which catalyzes the hydrolysis of ATP coupled CC with the electrogenic transport of potassium into the cytoplasm. CC This subunit is responsible for energy coupling to the transport CC system. {ECO:0000256|HAMAP-Rule:MF_00285}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + CC phosphate; Xref=Rhea:RHEA:16777, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.6; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00285, CC ECO:0000256|SAAS:SAAS01131062}; CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, CC KdpB and KdpC. {ECO:0000256|HAMAP-Rule:MF_00285, CC ECO:0000256|SAAS:SAAS00822521}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00285}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00285}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) CC (TC 3.A.3) family. Type IA subfamily. {ECO:0000256|HAMAP- CC Rule:MF_00285, ECO:0000256|SAAS:SAAS00822561}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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:0008556; F:potassium-transporting ATPase activity; IEA:UniProtKB-EC. 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 ECO:0000256|SAAS:SAAS00830384}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00822569}; KW Complete proteome {ECO:0000313|Proteomes:UP000257030}; KW Hydrolase {ECO:0000313|EMBL:REC77521.1}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00822424}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00830374}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00830366}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00822519}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00830373}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00285}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00822444}; KW Potassium transport {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00822397}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS01133003}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00830386}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00830383}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00822492}. FT TRANSMEM 35 56 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 62 83 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 222 242 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 254 277 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 583 602 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 614 635 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 655 678 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT NP_BIND 376 383 ATP. {ECO:0000256|HAMAP-Rule:MF_00285}. FT ACT_SITE 310 310 4-aspartylphosphate intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00285}. FT METAL 517 517 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT METAL 521 521 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT BINDING 347 347 ATP. {ECO:0000256|HAMAP-Rule:MF_00285}. FT BINDING 351 351 ATP. {ECO:0000256|HAMAP-Rule:MF_00285}. FT BINDING 394 394 ATP. {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 //