(data stored in ACNUC7421 zone)

SWISSPROT: A0KED4_AERHH

ID   A0KED4_AERHH            Unreviewed;       685 AA.
AC   A0KED4;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 112.
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:ABK36770.1};
GN   OrderedLocusNames=AHA_0016 {ECO:0000313|EMBL:ABK36770.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK36770.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK36770.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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:SAAS00987028}.
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 inner 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}.
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DR   EMBL; CP000462; ABK36770.1; -; Genomic_DNA.
DR   RefSeq; WP_011704061.1; NC_008570.1.
DR   RefSeq; YP_854545.1; NC_008570.1.
DR   STRING; 380703.AHA_0016; -.
DR   EnsemblBacteria; ABK36770; ABK36770; AHA_0016.
DR   GeneID; 4490528; -.
DR   KEGG; aha:AHA_0016; -.
DR   PATRIC; fig|380703.7.peg.16; -.
DR   eggNOG; ENOG4105C8X; Bacteria.
DR   eggNOG; COG2216; LUCA.
DR   HOGENOM; HOG000244113; -.
DR   KO; K01547; -.
DR   OMA; LQPFAHF; -.
DR   BioCyc; AHYD380703:G1G7B-16-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
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-transporting ATPase activity; IEA:UniProtKB-UniRule.
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; SSF81660; SSF81660; 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;
DR   PRODOM; A0KED4.
DR   SWISS-2DPAGE; A0KED4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830384};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00285};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822569};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Hydrolase {ECO:0000313|EMBL:ABK36770.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000000756};
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     38     57       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM     72     90       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    228    249       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    261    284       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    591    614       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    620    645       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    657    679       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   NP_BIND     381    388       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   ACT_SITE    314    314       4-aspartylphosphate intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   METAL       522    522       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   METAL       526    526       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   BINDING     351    351       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   BINDING     355    355       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   BINDING     399    399       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
SQ   SEQUENCE   685 AA;  72650 MW;  49EEA209441FCB55 CRC64;
     MSKSASMSTD TIQVKGKKQK SQILQAMVEA LYRFNPRALF GSPILFTLWL AAVMATLESL
     LGQPLSGVAP SLAWQLTAWL WLTLWFANFA ETLAEGRGKA RADSLKAGMS QLKARRVTSP
     QDDKGEWVPA TSLLKGDLVL VRSGEMIPAD GEVVAGIASV NEAAITGESA PVIRESGTDR
     SGVTGNTTVV SDQIWVHISN NPGESTLDRM IALVEGAKRQ KTPNEMALDA LLVGLTLIFL
     LVVATLPWFL DYNGTQVPRL YLLALFITLI PTTIGGLLSA IGIAGMDRLV KLNVIAKSGR
     AVEAAGDVRT LLLDKTGTIT FGNRMADELI PAPGVDPSLL AQAAMLASIG DNTPEGKSIL
     TLAGKSHTRP SQLESDIIIP FSAETRLSGL DRNGHHYRKG AVDAVLRYLS LDRKAVPELI
     LKSVDNIARQ GGTPLLVCTH EKLLGVVFLK DIIKPGIKAR FQILRHMGIR TVMITGDNPL
     TAAAIAAEAG VDDFIAEATP EKKLAYIRQE QADGRLVAMC GDGANDAPAL AQADVGLAMN
     EGTQAAKEAG NLVDLDSNPT KLLDVVLVGK QLLVTRGALT TFSIANDVAK YFAILPALFI
     AAYPQLGVLN LMQLGSPESA ILSAIIFNAL IIVALVPLAL RGVSLQGSAA SLLRRNLLIY
     GVGGLIVPFI GIKLIDLVIT GLGLV
//

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