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Database: UniProt
Entry: A0A429S4Y3_9ACTN
LinkDB: A0A429S4Y3_9ACTN
Original site: A0A429S4Y3_9ACTN 
ID   A0A429S4Y3_9ACTN        Unreviewed;       716 AA.
AC   A0A429S4Y3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 17.
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:RSS81735.1};
GN   ORFNames=EF918_09250 {ECO:0000313|EMBL:RSS81735.1};
OS   Streptomyces sp. WAC06614.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2487416 {ECO:0000313|EMBL:RSS81735.1, ECO:0000313|Proteomes:UP000277644};
RN   [1] {ECO:0000313|EMBL:RSS81735.1, ECO:0000313|Proteomes:UP000277644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC06614 {ECO:0000313|EMBL:RSS81735.1,
RC   ECO:0000313|Proteomes:UP000277644};
RA   Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT   "Unmasking the antibiotic production potential of Actinomycetes through
RT   CRISPR/Cas9 inactivate of ubiquitous gene clusters.";
RL   Submitted (NOV-2018) 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:RSS81735.1}.
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DR   EMBL; RPRY01000045; RSS81735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A429S4Y3; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000277644; 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   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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:RSS81735.1};
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:UP000277644};
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        60..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        243..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        278..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        617..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        647..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        689..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        331
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   BINDING         368
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   BINDING         372
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   BINDING         401..408
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   BINDING         424
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   BINDING         551
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   BINDING         555
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
SQ   SEQUENCE   716 AA;  75205 MW;  FA542BA2B26AC980 CRC64;
     MPPAAAQHVP PGLGTPPRTP INRPSRKRSG QVNLVDPELL AASAREAVGK LHPRELVKKP
     VLFVVAVGSV LTTLSALIHP SVFTWVISVW LWLTVLFANL AEAVAEGRGR AQAESLRKAR
     TDTVAVRLNH WTYGANLRHA ETEVVTPAEL QPFDFVVVEA GELIPADGDV VDGAAMVDES
     AVTGESAPVL REAGGDRSGV TGGTTVLSDS VVVRVTSRPG HSFIDRMIAL VEGATRQKTP
     NEIALNILLA ALTVIFILVV VAIQPMADYA HAAQSTTVLV ALLVTLIPTT IGALLSAIGI
     AGMDRLVQRN VIAMSGRAVE AAGDVNTLLL DKTGTITLGN REAAAFIPLP GVDHLKVAEA
     AQLSSLADET PEGRSVVALA HQYGLQPAAV GDLSNPRFTE FSARTRMSGI NLSWDNGAGC
     AIRKGATAQV CDWVTMRGGT VPPEAEAWSA TVSESGGTPL LVAVHDWDGP RVLGIIHLKD
     VVKEGIRERF AELRSMGIRT VMVTGDNELT ARAIAAEAGV DEYLAEATPE DKLALIKREQ
     AGGKLVAMTG DGTNDAPALA QADVGVAMNT GTSAAKEAGN MVDLDSNPTK LIEIVEIGKQ
     LLITRGALTT FSITNDVAKY FAIIPAMFTA AYPGLEALNI MGLSSPTSAI TSAIIFNALI
     IIALIPLALR GVRYKPASAH DLLRRNLRVY GLGGLVLPFV GIKLIDLLVS TIPGLG
//
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