ID A4FMI6_SACEN Unreviewed; 691 AA.
AC A4FMI6;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 120.
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:CAM05261.1};
GN OrderedLocusNames=SACE_6088 {ECO:0000313|EMBL:CAM05261.1};
GN ORFNames=A8924_6435 {ECO:0000313|EMBL:PFG98909.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM05261.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM05261.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC {ECO:0000313|EMBL:CAM05261.1};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [2] {ECO:0000313|EMBL:PFG98909.1, ECO:0000313|Proteomes:UP000225825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG98909.1,
RC ECO:0000313|Proteomes:UP000225825};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (SEP-2017) 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}.
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DR EMBL; AM420293; CAM05261.1; -; Genomic_DNA.
DR EMBL; PDBV01000001; PFG98909.1; -; Genomic_DNA.
DR RefSeq; WP_009947573.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FMI6; -.
DR STRING; 405948.SACE_6088; -.
DR KEGG; sen:SACE_6088; -.
DR eggNOG; COG2216; Bacteria.
DR HOGENOM; CLU_025728_2_0_11; -.
DR OMA; ILWLWFT; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000006728; Chromosome.
DR Proteomes; UP000225825; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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:CAM05261.1};
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:UP000006728};
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 47..67
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 225..249
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 255..282
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 592..610
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 662..680
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT ACT_SITE 313
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 384..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
SQ SEQUENCE 691 AA; 72591 MW; CC5DEC9AA43D28D8 CRC64;
MTTTLEKPAR RQEVPAARKL TAGAFSPRQL LTSLPDALRK LNPRHQLANP VMFVVWVGSV
LVTVLTLLEP NGFSIAVALW LWFTVLFANL AEAVAEGRGR AQAESLRRTK TEAVARRLAD
DGTEEDVPGN ALRVGDRVVV EAGQVIPGDG DVIEGIATVD ESAITGESAP VIRESGGDRS
AVTAGTTVLS DRIVVRITTK PGETFVDRMI ALVEGAQRQK TPNEIALTIL LSTLTIIFVL
AVLALQPMAG YSGGLLSVVV LTALLVCLIP TTIGALLSAI GIAGMDRLVQ RNVLAKSGRA
VEAAGDVNTL LLDKTGTITY GNRQATELIP VGEVTKGELA AVARLSSLAD ETPEGVSIVT
YCAENFGLPG EAQAEELAAD AVAFTAQTRM SGIDIGGRQI RKGAASAVRQ WTSGPVPSEV
DTVVDEISAQ GGTPLVVAEC SGGTTRVLGV VRLSDVVKPG MKERFAELRA MGIRTVMVTG
DNPLTAKAIA AEAGVDDFLA EAKPEDKMEL IRREQEGGRL VAMTGDGTND APALAQADVG
VAMNTGTAAA KEAGNMVDLD SDPTKLIEIV EIGKQMLITR GALTTFSIAN DLAKYFAILP
AMFVAIHPQL DALNIMRLAT PTSAILSAVV FNALIIVALI PLALRGVRYR PMSAASLLRR
NLLVYGLGGI ATPFAGIWLI DLLVRFVPGI G
//