ID A0A0F5BIQ4_ENTCL Unreviewed; 682 AA. AC A0A0F5BIQ4; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 09-DEC-2015, entry version 6. DE SubName: Full=Potassium-transporting ATPase subunit B {ECO:0000313|EMBL:KJW97023.1}; DE EC=3.6.3.12 {ECO:0000313|EMBL:KJW97023.1}; GN ORFNames=RZ87_15255 {ECO:0000313|EMBL:KJW97023.1}; OS Enterobacter cloacae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=550 {ECO:0000313|EMBL:KJW97023.1, ECO:0000313|Proteomes:UP000033606}; RN [1] {ECO:0000313|EMBL:KJW97023.1, ECO:0000313|Proteomes:UP000033606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIDEIMsCOL1 {ECO:0000313|EMBL:KJW97023.1, RC ECO:0000313|Proteomes:UP000033606}; RA Adams M., Sutton G., Nelson K., Bonomo R., McCorrison J., Sanka R., RA Brinkac L., Nierman W.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. 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|SAAS:SAAS00347917}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + K(+)(Out) = ADP + phosphate + CC K(+)(In). {ECO:0000256|SAAS:SAAS00347936}. CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, CC KdpB and KdpC. {ECO:0000256|SAAS:SAAS00348102}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|SAAS:SAAS00347925}; Multi-pass membrane protein CC {ECO:0000256|SAAS:SAAS00347925}. 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:KJW97023.1}. 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; JZKL01000028; KJW97023.1; -; Genomic_DNA. DR RefSeq; WP_008501077.1; NZ_JZKL01000028.1. DR EnsemblBacteria; KJW97023; KJW97023; RZ87_15255. DR Proteomes; UP000033606; Unassembled WGS sequence. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008556; F:potassium-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 2.70.150.10; -; 1. DR Gene3D; 3.40.1110.10; -; 1. DR Gene3D; 3.40.50.1000; -; 2. DR HAMAP; MF_00285; KdpB; 1. DR InterPro; IPR023299; ATPase_P-typ_cyto_domN. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006391; P-type_ATPase_bsu_IA. DR InterPro; IPR001757; P_typ_ATPase. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00119; CATATPASE. DR SUPFAM; SSF56784; SSF56784; 3. 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|SAAS:SAAS00077701}; KW Cell inner membrane {ECO:0000256|SAAS:SAAS00308955}; KW Cell membrane {ECO:0000256|SAAS:SAAS00018096}; KW Complete proteome {ECO:0000313|Proteomes:UP000033606}; KW Hydrolase {ECO:0000256|SAAS:SAAS00077601, KW ECO:0000313|EMBL:KJW97023.1}; KW Ion transport {ECO:0000256|SAAS:SAAS00017979}; KW Magnesium {ECO:0000256|SAAS:SAAS00077675}; KW Membrane {ECO:0000256|SAAS:SAAS00077633}; KW Metal-binding {ECO:0000256|SAAS:SAAS00017755}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00077613}; KW Potassium {ECO:0000256|SAAS:SAAS00018065}; KW Potassium transport {ECO:0000256|SAAS:SAAS00018976}; KW Transmembrane {ECO:0000256|SAAS:SAAS00077579}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00077548}; KW Transport {ECO:0000256|SAAS:SAAS00017788}. FT DOMAIN 72 296 E1-E2_ATPase. {ECO:0000259|Pfam:PF00122}. FT DOMAIN 301 530 Hydrolase. {ECO:0000259|Pfam:PF00702}. 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 //