ID D4YJT4_9MICO Unreviewed; 691 AA.
AC D4YJT4;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 73.
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:EFG48504.1};
GN ORFNames=HMPREF0183_0194 {ECO:0000313|EMBL:EFG48504.1};
OS Brevibacterium mcbrellneri ATCC 49030.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=585530 {ECO:0000313|EMBL:EFG48504.1, ECO:0000313|Proteomes:UP000005714};
RN [1] {ECO:0000313|EMBL:EFG48504.1, ECO:0000313|Proteomes:UP000005714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49030 {ECO:0000313|EMBL:EFG48504.1,
RC ECO:0000313|Proteomes:UP000005714};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2010) 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 and for the
CC release of the potassium ions to the cytoplasm. {ECO:0000256|HAMAP-
CC 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|ARBA:ARBA00004651,
CC ECO:0000256|HAMAP-Rule:MF_00285}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, 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:EFG48504.1}.
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DR EMBL; ADNU01000008; EFG48504.1; -; Genomic_DNA.
DR RefSeq; WP_005881798.1; NZ_ADNU01000008.1.
DR AlphaFoldDB; D4YJT4; -.
DR STRING; 585530.HMPREF0183_0194; -.
DR eggNOG; COG2216; Bacteria.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000005714; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR CDD; cd02078; P-type_ATPase_K; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR023214; HAD_sf.
DR InterPro; IPR006391; P-type_ATPase_bsu_IA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01497; kdpB; 1.
DR PANTHER; PTHR43743; POTASSIUM-TRANSPORTING ATPASE ATP-BINDING SUBUNIT; 1.
DR PANTHER; PTHR43743:SF1; POTASSIUM-TRANSPORTING ATPASE ATP-BINDING SUBUNIT; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 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}; Hydrolase {ECO:0000313|EMBL:EFG48504.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00285};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00285};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00285};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00285};
KW 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}; Reference proteome {ECO:0000313|Proteomes:UP000005714};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW 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 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 71..88
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 222..243
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 255..279
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 596..619
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 665..688
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT REGION 98..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 381..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 527
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
SQ SEQUENCE 691 AA; 72919 MW; C713DAE0CAA3686C CRC64;
MTTQIQETET ETRDATSAQS GISGKLILAS LPQALRKLNP ATMVRTPVMF IVEVGAAITL
VLGFIHPSLF TFTLAIWLFL TVVFANLAEA VAEGRGKAQA DALRKTQTAS TGRVRRPNGE
VEEVPSSSLR PGDVVIVSAG ETIPGDGDVI AGAATVDESA VTGESAPVIR ESGGDRSAVT
GGTRVLSDTI EVRITSEPGN TFIDRMIGLV EGASRQKTPN ELALSAFLSV LTLIFVLVVL
TLVPMANYSN AQQPITVLIA LLVCLIPTTI GALLSAIGIA GMDRLIKRNV LATSGKAVEA
AGDVTTLLLD KTGTITVGNR KATAFVAAEG ISEIELARKA QLSSLADETP EGRSIVVLAQ
DGLGLGEVPE ADFAQAEFIP FSAETRMSGV KLSDNHQVVK GAATEMVKWV EQSGVKVGDD
VKHAIERISN DGGTALVVAE EENEKRQVLG TIHLKDIIKE GMVERFKTLR SMGIRTVMIT
GDNELTALAI AREAGVDDYL AQAKPEDKLA LIRREQKGGN MVAMTGDGTN DAPALAQADV
GVAMNTGTQA AKEAGNMVDL DSDPTKLIEI VEIGKQLLIT RGALTTFSIA NDIAKYFAIV
PAMFVVAFPG LDVLNIMRLS SPESAITSAV IFNAIIIVLL IPLALRGVKY VPGTSHQLLR
RNLVVYGLGG FVVPFIGIKI IDMIVSLLPG F
//
