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Potassium-transporting ATPase ATP-binding subunit (EC 3.6.3.12) (ATP phosphohydrolase [potassium-transporting] B chain) (Potassium-binding and translocating subunit B) (Potassium-translocating ATPase B chain)

 A0A0L6JDM5_9RHIZ        Unreviewed;       696 AA.
A0A0L6JDM5;
11-NOV-2015, integrated into UniProtKB/TrEMBL.
11-NOV-2015, sequence version 1.
25-OCT-2017, entry version 13.
RecName: Full=Potassium-transporting ATPase ATP-binding subunit {ECO:0000256|HAMAP-Rule:MF_00285};
EC=3.6.3.12 {ECO:0000256|HAMAP-Rule:MF_00285};
AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain {ECO:0000256|HAMAP-Rule:MF_00285};
AltName: Full=Potassium-binding and translocating subunit B {ECO:0000256|HAMAP-Rule:MF_00285};
AltName: Full=Potassium-translocating ATPase B chain {ECO:0000256|HAMAP-Rule:MF_00285};
Name=kdpB {ECO:0000256|HAMAP-Rule:MF_00285};
ORFNames=AKJ13_04640 {ECO:0000313|EMBL:KNY23778.1};
Methylobacterium sp. ARG-1.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Methylobacteriaceae; Methylobacterium.
NCBI_TaxID=1692501 {ECO:0000313|EMBL:KNY23778.1, ECO:0000313|Proteomes:UP000036734};
[1] {ECO:0000313|Proteomes:UP000036734}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ARG-1 {ECO:0000313|Proteomes:UP000036734};
Hirst R., James-Pederson M., Tai A.;
"Draft Genome Sequence of Methylobacterium sp. Strain ARG-1 Isolated
from the White-Rot Fungus, Armillaria gallica.";
Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Part of the high-affinity ATP-driven potassium transport
(or Kdp) system, which catalyzes the hydrolysis of ATP coupled
with the electrogenic transport of potassium into the cytoplasm.
This subunit is responsible for energy coupling to the transport
system. {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00822527}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + K(+)(Out) = ADP + phosphate +
K(+)(In). {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00822523}.
-!- SUBUNIT: The system is composed of three essential subunits: KdpA,
KdpB and KdpC. {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00822521}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
Rule:MF_00285}; Multi-pass membrane protein {ECO:0000256|HAMAP-
Rule:MF_00285}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IA subfamily. {ECO:0000256|HAMAP-
Rule:MF_00285, ECO:0000256|SAAS:SAAS00822561}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KNY23778.1}.
-----------------------------------------------------------------------
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EMBL; LHCD01000003; KNY23778.1; -; Genomic_DNA.
RefSeq; WP_050732303.1; NZ_LHCD01000003.1.
EnsemblBacteria; KNY23778; KNY23778; AKJ13_04640.
PATRIC; fig|1692501.3.peg.3384; -.
Proteomes; UP000036734; Unassembled WGS sequence.
GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0008556; F:potassium-transporting ATPase activity; IEA:UniProtKB-UniRule.
CDD; cd02078; P-type_ATPase_K; 1.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
HAMAP; MF_00285; KdpB; 1.
InterPro; IPR023299; ATPase_P-typ_cyto_domN.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006391; P-type_ATPase_bsu_IA.
InterPro; IPR001757; P_typ_ATPase.
SUPFAM; SSF56784; SSF56784; 3.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 2.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
TIGRFAMs; TIGR01497; kdpB; 1.
PROSITE; PS00154; ATPASE_E1_E2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00830384};
Cell membrane {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00822569};
Complete proteome {ECO:0000313|Proteomes:UP000036734};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00830376, ECO:0000313|EMBL:KNY23778.1};
Ion transport {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00822397};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00830374};
Membrane {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00822569, ECO:0000256|SAAS:SAAS00830383};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00830368};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00830384};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00285};
Potassium {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00822397};
Potassium transport {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00822397};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00830383};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00830383};
Transport {ECO:0000256|HAMAP-Rule:MF_00285,
ECO:0000256|SAAS:SAAS00822397}.
TRANSMEM 33 51 Helical. {ECO:0000256|HAMAP-
Rule:MF_00285}.
TRANSMEM 63 81 Helical. {ECO:0000256|HAMAP-
Rule:MF_00285}.
TRANSMEM 216 240 Helical. {ECO:0000256|HAMAP-
Rule:MF_00285}.
TRANSMEM 246 271 Helical. {ECO:0000256|HAMAP-
Rule:MF_00285}.
TRANSMEM 598 616 Helical. {ECO:0000256|HAMAP-
Rule:MF_00285}.
TRANSMEM 628 648 Helical. {ECO:0000256|HAMAP-
Rule:MF_00285}.
TRANSMEM 668 686 Helical. {ECO:0000256|HAMAP-
Rule:MF_00285}.
NP_BIND 374 381 ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
ACT_SITE 304 304 4-aspartylphosphate intermediate.
{ECO:0000256|HAMAP-Rule:MF_00285}.
METAL 532 532 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00285}.
METAL 536 536 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00285}.
BINDING 341 341 ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
BINDING 345 345 ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
BINDING 392 392 ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
SEQUENCE 696 AA; 72402 MW; B0E2F05B4FC07EED CRC64;
MSRKTASLFS PALVGPALLG SGKKLDPRAM IRNPVMFVVE VVAALTTFLF LRDVATGAGD
LLFSGQIILW LWFTLVFANF AEALAEGRGK AQADSLRRTR TEMMAKRLTG PDESYETVPG
TSLKVGDVVL VEAGELIPSD GEVIQGVASV NEAAITGESA PVIRESGGDR SAVTGGTQVL
SDQIRVRITA AAGSTFVDRM IALVEGASRQ KTPNEIALNI LLAGLTIVFV FAVASIPSFA
AYAGGAIPLI VLVALFVTLI PTTIGALLSA IGIAGMDRLV RFNVLALSGR AVEAAGDVDT
LLLDKTGTIT LGNRQATEFR PVSGVTEADL ADAAQLASLA DETPEGRSIV VLAKEAYGIR
ARDMAGLNAS FVPFTAQSRM SGVDLDGVSI RKGAVEAVIA SVSAQPMASR GSNAALAYQP
EAEPESVAEI RAIAEEIAKA GGTPLAVARD GRLLGVVYLK DIVKGGIRER FAELRRMGIR
TVMITGDNPM TAAAIAAEAG VDDFLAQATP EDKLALIRTE QMQGKLVAMC GDGTNDAPAL
AQADVGVAMN TGTVAAREAG NMVDLDSDPT KLIEIVGIGK QLLMTRGALT TFSIANDVAK
YFAIIPAMFL GLYPQLQALN VMGLASPQSA ILSAIIFNAL IIVALIPLAL RGVTYRAVGA
AALLRRNLLI YGLGGVLVPF AAIKAIDLAV TALHLA


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