ID V3E054_ENTCL Unreviewed; 682 AA. AC V3E054; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 26-NOV-2014, entry version 8. DE RecName: Full=Potassium-transporting ATPase B chain {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}; RN [1] {ECO:0000313|EMBL:ESL83116.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UCICRE 12 {ECO:0000313|EMBL:ESL83116.1}; 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: One of the components of the high-affinity ATP-driven CC potassium transport (or KDP) system, which catalyzes the CC hydrolysis of ATP coupled with the exchange of hydrogen and CC potassium ions. {ECO:0000256|HAMAP-Rule:MF_00285, CC ECO:0000256|SAAS:SAAS00018086}. 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 -!- 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 EnsemblBacteria; ESL83116; ESL83116; L423_01377. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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; IPR001757; Cation_transp_P_typ_ATPase. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006391; K-transp_ATPase_bsu_IA. 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|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00077701}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00018096}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00077601}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00017979}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00077675}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00077633}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00017755}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00077613}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00017910}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00018065}; KW Potassium transport {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00018976}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00077579}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00077548}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00285, KW ECO:0000256|SAAS:SAAS00017788}. 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 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}. 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 //