ID V3E054_9ENTR Unreviewed; 682 AA. AC V3E054; A0A384HQJ8; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 12-AUG-2020, entry version 47. 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 ORFNames=ASU87_13650 {ECO:0000313|EMBL:KTJ34877.1}; OS Enterobacter roggenkampii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=1812935 {ECO:0000313|EMBL:KTJ34877.1, ECO:0000313|Proteomes:UP000053549}; RN [1] {ECO:0000313|EMBL:KTJ34877.1, ECO:0000313|Proteomes:UP000053549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SMART_454 {ECO:0000313|EMBL:KTJ34877.1, RC ECO:0000313|Proteomes:UP000053549}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. 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:KTJ34877.1}. 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; LPPZ01000013; KTJ34877.1; -; Genomic_DNA. DR RefSeq; WP_008501077.1; NZ_VLNP01000012.1. DR EnsemblBacteria; ESL83116; ESL83116; L423_01377. DR KEGG; ecls:LI67_007225; -. DR HOGENOM; CLU_025728_2_0_6; -. DR KO; K01547; -. DR Proteomes; UP000053549; 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: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 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; 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}; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00285}; 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}; Translocase {ECO:0000256|HAMAP-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..82 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 219..242 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 248..274 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 584..602 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 614..636 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT TRANSMEM 656..681 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT NP_BIND 377..384 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT ACT_SITE 307 FT /note="4-aspartylphosphate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT METAL 518 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT METAL 522 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT BINDING 344 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT BINDING 348 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" FT BINDING 395 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285" SQ SEQUENCE 682 AA; 72345 MW; 898ECA82203CFDA3 CRC64; MSRKQLALFE PSLVRQALMD AVKKLSPRVQ WHNPVMFIVW AGSVLTTALA IAMGTGHMPG NAMFTGAISL WLWFTVLFAN FAEALAEGRS KAQANSLKGV KKTAFARKLR EPKYGAQMDH VPADELRKGD VVLVEAGDII PCDGEVIEGG ASVDESAITG ESAPVIRESG GDFASVTGGT RILSDWLVIQ CSVNPGETFL DRMIAMVEGA QRRKTPNEIA LTILLVALTI VFLLATATLW PFSAYGGTAV TVTVLVALLV CLIPTTIGGL LSAIGVAGMS RMLGANVIAT SGRAVEAAGD VDVLLLDKTG TITLGNRQAS DFLPAPGVDE KTLADAAQLS SLADETPEGR SIVILAKQRF NLRQRDVQSL HATFVPFTAQ TRMSGINIQD RMIRKGSVDA IRRHIEANNG HFPPEVDSLV ESVARQGATP LVVAEGARVL GVIALKDIVK GGIKERFAQL RKMGIKTVMI TGDNRLTAAA IAAEAGVDDF LSEATPEAKL ALIRQYQAEG RLVAMTGDGT NDAPALAQAD VAVAMNSGTQ AAKEAGNMVD LDSNPTKLIE VVHIGKQMLM TRGSLTTFSI ANDVAKYFAI IPAAFAATYP QLNALNVMHL HSPASAILSA VIFNALIIVF LIPLALKGVS YKPLTAAAML RRNLWIYGLG GLVVPFVGIK VIDLLLTLFG LV //