(data stored in SCRATCH zone)

SWISSPROT: B8I9I7_METNO

ID   B8I9I7_METNO            Unreviewed;       701 AA.
AC   B8I9I7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAY-2019, entry version 80.
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   OrderedLocusNames=Mnod_0195 {ECO:0000313|EMBL:ACL55240.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55240.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55240.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the high-affinity ATP-driven potassium transport
CC       (or Kdp) system, which catalyzes the hydrolysis of ATP coupled
CC       with the electrogenic transport of potassium into the cytoplasm.
CC       This subunit is responsible for energy coupling to the transport
CC       system. {ECO:0000256|HAMAP-Rule:MF_00285}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) +
CC         phosphate; Xref=Rhea:RHEA:16777, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00285,
CC         ECO:0000256|SAAS:SAAS01131062};
CC   -!- SUBUNIT: The system is composed of three essential subunits: KdpA,
CC       KdpB and KdpC. {ECO:0000256|HAMAP-Rule:MF_00285,
CC       ECO:0000256|SAAS:SAAS00822521}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00285}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00285}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IA subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00285, ECO:0000256|SAAS:SAAS00822561}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00285}.
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DR   EMBL; CP001349; ACL55240.1; -; Genomic_DNA.
DR   RefSeq; WP_015926953.1; NC_011894.1.
DR   STRING; 460265.Mnod_0195; -.
DR   EnsemblBacteria; ACL55240; ACL55240; Mnod_0195.
DR   KEGG; mno:Mnod_0195; -.
DR   eggNOG; ENOG4105C8X; Bacteria.
DR   eggNOG; COG2216; LUCA.
DR   HOGENOM; HOG000244113; -.
DR   KO; K01547; -.
DR   OMA; ILWLWFT; -.
DR   OrthoDB; 237367at2; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008556; F:potassium-transporting ATPase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02078; P-type_ATPase_K; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 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   PANTHER; PTHR43743; PTHR43743; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   TIGRFAMs; TIGR01497; kdpB; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B8I9I7.
DR   SWISS-2DPAGE; B8I9I7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830384};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00285};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822569};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822424};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830374};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830366};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822519};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830373};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00285};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822444};
KW   Potassium transport {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822397};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS01133003};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830386};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830383};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822492}.
FT   TRANSMEM      6     23       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM     35     55       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM     61     81       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    223    247       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    253    278       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    605    623       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    635    657       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    677    700       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   NP_BIND     381    388       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   ACT_SITE    311    311       4-aspartylphosphate intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   METAL       539    539       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   METAL       543    543       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   BINDING     348    348       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   BINDING     352    352       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   BINDING     399    399       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
SQ   SEQUENCE   701 AA;  73061 MW;  723E8A42C5782F95 CRC64;
     MARQISSLFS AALIGPALIG AVRKLDPRIL IRNPVMFVVE VVAALTTVLF VRDVLTGGAD
     LAFTGQIILW LWFTVLFANF AEAIAEGRGK AQADALRRTR TEMTAKLLTG PAASVGGPRS
     GFRVVPGTTL RVGDVVLVEA GDLIPSDGEV IEGVASVNEA AITGESAPVI RESGGDRSAV
     TGGTQVLSDW IRVRITAAAG STFVDRMIAL VEGAARQKTP NEIALNILLA GLTIIFVIAV
     ATIPSFAAYA GGAIPMVVLV ALFVTLIPTT IGALLSAIGI AGMDRLVRFN VLAMSGRAVE
     AAGDVDTLLL DKTGTITLGN RQAAEFRPLR GVTEQELADA AQLASLADET PEGRSIVVLT
     KERYGIRARD MASLHATFVP FTAQSRMSGV DLDGSSIRKG AVDAILAHVT ASATAVVPSG
     AIRVMQPQVS AAAVREVQAI TEEIAKAGGT PLAVARGGRL LGVVHLKDIV KGGIRERFAE
     LRRMGIRTVM ITGDNPVTAA AIAAEAGVDD FLAQATPEDK LALIRKEQQQ GKLVAMCGDG
     TNDAPALAQA DVGVAMNTGT VAAREAGNMV DLDSDPTKLI EIVEIGKQLL MTRGALTTFS
     IANDVAKYFA IIPAMFVTLY PQLQALNVMG LASPQSAILS AIIFNALIIV ALIPLALKGV
     RYRAVGAAAL LRRNLMIYGL GGILVPFAGI KLIDLAVSAL L
//

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