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Database: UniProt
Entry: A0A0Q5UVQ8_9FLAO
LinkDB: A0A0Q5UVQ8_9FLAO
Original site: A0A0Q5UVQ8_9FLAO 
ID   A0A0Q5UVQ8_9FLAO        Unreviewed;       681 AA.
AC   A0A0Q5UVQ8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ORFNames=ASG38_02420 {ECO:0000313|EMBL:KQS53603.1};
OS   Flavobacterium sp. Leaf359.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1736351 {ECO:0000313|EMBL:KQS53603.1, ECO:0000313|Proteomes:UP000051024};
RN   [1] {ECO:0000313|Proteomes:UP000051024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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|HAMAP-Rule:MF_00285};
CC       Multi-pass membrane protein {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:KQS53603.1}.
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DR   EMBL; LMPW01000001; KQS53603.1; -; Genomic_DNA.
DR   RefSeq; WP_056066612.1; NZ_LMPW01000001.1.
DR   AlphaFoldDB; A0A0Q5UVQ8; -.
DR   STRING; 1736351.ASG38_02420; -.
DR   OrthoDB; 1521937at2; -.
DR   Proteomes; UP000051024; 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.
DR   PROSITE; PS01229; COF_2; 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};
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:UP000051024};
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        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        222..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        251..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        588..611
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        617..637
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   TRANSMEM        657..680
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
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         377..384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   BINDING         396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   BINDING         519
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT   BINDING         523
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
SQ   SEQUENCE   681 AA;  73144 MW;  857117942DC92DBB CRC64;
     MKTQNKSLFQ KELLKEAFVQ SFLKLNPANL FRNPIMFTVE IGTVVMLCVC LWILTGEQSQ
     GSFVYNFTVF IILLFTLLFA NFAEAIAEAR GKAQADSLRK TREETPAKKI FPVGEMYVDE
     LQIVPSSSLV KGDIFICEAG DTIPTDGEII EGLATIDESA ITGESAPVIR EAGGDKSSVT
     GGTKVLSDKI KVRVTTEPGE SFLDKMIALV EGASRQKTPN EIALTILLAG FTLVFIIVCT
     TLKPFADYAN ITITIASFIS LFVCLIPTTI GGLLSAIGIA GMDRALRANV ITKSGKAVET
     AGDIDVLLLD KTGTITIGNR KATQFYPTAG ISEQEFIKAS ILSSLADETP EGKSIIELAG
     KEATKNLSIE GATLIKFTAE TRSSGVTLPD GTRIRKGAYD AIRKLSEKAG NTFPNDTSDR
     VTEISSNGGT PLVVSENDKV LGVIELQDII KPGIQERFER LRRMGVKTVM VTGDNPLTAK
     FIAEKAGVDD FIAEAKPEDK MNYIKNEQIK GKLVAMMGDG TNDAPALAQA DVGVAMNSGT
     QAAKEAGNMV DLDNDPTKLI EIVEIGKQLL MTRGTLTTFS IANDVAKYFA IIPALFITAI
     PALQGLNIMH LHSPESAILS AVIFNAVVIP FLIPLALKGV TYKPIGASAL LRRNLLFYGL
     GGIIVPFIGI KIIDMIVTLF I
//
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