ID V3E054_ENTCL Unreviewed; 682 AA. AC V3E054; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 13-APR-2016, entry version 19. DE RecName: Full=Potassium-transporting ATPase ATP-binding subunit {ECO:0000256|HAMAP-Rule:MF_00285}; DE EC=3.6.3.12 {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=L423_01377 {ECO:0000313|EMBL:ESL83116.1}; OS Enterobacter cloacae UCICRE 12. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=1329856 {ECO:0000313|EMBL:ESL83116.1, ECO:0000313|Proteomes:UP000017344}; RN [1] {ECO:0000313|EMBL:ESL83116.1, ECO:0000313|Proteomes:UP000017344} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCICRE 12 {ECO:0000313|EMBL:ESL83116.1, RC ECO:0000313|Proteomes:UP000017344}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Murphy C., Cosimi L., Cerqueira G., Feldgarden M., Hung D., RA Onderdonk A.B., Ferraro M.J., Hooper D., Dekker J., O'Brien T., RA Huang S., Quan V., Ernst C., Delaney M., DuBois A., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., RA Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., RA Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterobacter cloacae UCI 12."; RL Submitted (SEP-2013) 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|HAMAP-Rule:MF_00285, CC ECO:0000256|SAAS:SAAS00308962}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + K(+)(Out) = ADP + phosphate + CC K(+)(In). {ECO:0000256|HAMAP-Rule:MF_00285, CC ECO:0000256|SAAS:SAAS00019083}. 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:SAAS00308966}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|SAAS:SAAS00498797}; Multi-pass membrane protein CC {ECO:0000256|SAAS:SAAS00498797}. 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) (TC CC 3.A.3) family. Type IA subfamily. {ECO:0000256|HAMAP- CC Rule:MF_00285}. 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:ESL83116.1}. 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; AYID01000001; ESL83116.1; -; Genomic_DNA. DR RefSeq; WP_008501077.1; NZ_KI535461.1. DR EnsemblBacteria; ESL83116; ESL83116; L423_01377. DR Proteomes; UP000017344; 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 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|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00455152}; KW Cell inner membrane {ECO:0000256|SAAS:SAAS00498759}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00427192}; KW Complete proteome {ECO:0000313|Proteomes:UP000017344}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00455106}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00426661}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00426691}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00455173}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00427147}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00455177}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00285}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00426669}; KW Potassium transport {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00426911}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00455121}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00455137}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00426959}. FT TRANSMEM 34 54 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 62 82 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 219 239 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 254 274 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 588 608 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 616 636 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT TRANSMEM 662 682 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT DOMAIN 72 296 E1-E2_ATPase. {ECO:0000259|Pfam:PF00122}. FT NP_BIND 377 384 ATP. {ECO:0000256|HAMAP-Rule:MF_00285}. FT ACT_SITE 307 307 4-aspartylphosphate intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00285}. FT METAL 518 518 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT METAL 522 522 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00285}. FT BINDING 344 344 ATP. {ECO:0000256|HAMAP-Rule:MF_00285}. FT BINDING 348 348 ATP. {ECO:0000256|HAMAP-Rule:MF_00285}. FT BINDING 395 395 ATP. {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 //