KDPB_ECOLI
ID KDPB_ECOLI Reviewed; 682 AA.
AC P03960; P78053; P78145;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Potassium-transporting ATPase ATP-binding subunit {ECO:0000255|HAMAP-Rule:MF_00285};
DE EC=7.2.2.6 {ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:34272288};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain {ECO:0000255|HAMAP-Rule:MF_00285};
DE AltName: Full=Potassium-binding and translocating subunit B {ECO:0000255|HAMAP-Rule:MF_00285};
DE AltName: Full=Potassium-translocating ATPase B chain {ECO:0000255|HAMAP-Rule:MF_00285};
GN Name=kdpB {ECO:0000255|HAMAP-Rule:MF_00285};
GN OrderedLocusNames=b0697, JW0685;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6146979; DOI=10.1073/pnas.81.15.4746;
RA Hesse J.E., Wieczorek L., Altendorf K., Reicin A.S., Dorus E., Epstein W.;
RT "Sequence homology between two membrane transport ATPases, the Kdp-ATPase
RT of Escherichia coli and the Ca2+-ATPase of sarcoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4746-4750(1984).
RN [2]
RP SEQUENCE REVISION TO 274-275 AND 456.
RA Epstein W.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION IN POTASSIUM TRANSPORT, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=2849541; DOI=10.1111/j.1432-1033.1988.tb14438.x;
RA Siebers A., Altendorf K.;
RT "The K+-translocating Kdp-ATPase from Escherichia coli. Purification,
RT enzymatic properties and production of complex- and subunit-specific
RT antisera.";
RL Eur. J. Biochem. 178:131-140(1988).
RN [7]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=1532387; DOI=10.1128/jb.174.7.2145-2151.1992;
RA Polarek J.W., Williams G., Epstein W.;
RT "The products of the kdpDE operon are required for expression of the Kdp
RT ATPase of Escherichia coli.";
RL J. Bacteriol. 174:2145-2151(1992).
RN [8]
RP ACTIVE SITE, AND MUTAGENESIS OF ASP-300 AND ASP-307.
RX PubMed=1474895; DOI=10.1111/j.1365-2958.1992.tb01786.x;
RA Puppe W., Siebers A., Altendorf K.;
RT "The phosphorylation site of the Kdp-ATPase of Escherichia coli: site-
RT directed mutagenesis of the aspartic acid residues 300 and 307 of the KdpB
RT subunit.";
RL Mol. Microbiol. 6:3511-3520(1992).
RN [9]
RP FUNCTION IN POTASSIUM TRANSPORT.
RC STRAIN=K12;
RX PubMed=8499455; DOI=10.1016/0005-2728(93)90216-3;
RA Kollmann R., Altendorf K.;
RT "ATP-driven potassium transport in right-side-out membrane vesicles via the
RT Kdp system of Escherichia coli.";
RL Biochim. Biophys. Acta 1143:62-66(1993).
RN [10]
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=9858692; DOI=10.1016/s0005-2736(98)00179-5;
RA Gassel M., Siebers A., Epstein W., Altendorf K.;
RT "Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of
RT Escherichia coli.";
RL Biochim. Biophys. Acta 1415:77-84(1998).
RN [11]
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=10608856; DOI=10.1074/jbc.274.53.37901;
RA Gassel M., Mollenkamp T., Puppe W., Altendorf K.;
RT "The KdpF subunit is part of the K(+)-translocating Kdp complex of
RT Escherichia coli and is responsible for stabilization of the complex in
RT vitro.";
RL J. Biol. Chem. 274:37901-37907(1999).
RN [12]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [13]
RP SUBUNIT.
RX PubMed=18298081; DOI=10.1021/bi702038e;
RA Heitkamp T., Kalinowski R., Boettcher B., Boersch M., Altendorf K.,
RA Greie J.C.;
RT "K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a
RT functional and structural dimer.";
RL Biochemistry 47:3564-3575(2008).
RN [14]
RP FUNCTION.
RX PubMed=23930894; DOI=10.1021/bi400729e;
RA Damnjanovic B., Weber A., Potschies M., Greie J.C., Apell H.J.;
RT "Mechanistic analysis of the pump cycle of the KdpFABC P-type ATPase.";
RL Biochemistry 52:5563-5576(2013).
RN [15] {ECO:0007744|PDB:1SVJ, ECO:0007744|PDB:1U7Q}
RP STRUCTURE BY NMR OF 316-451.
RX PubMed=15364580; DOI=10.1016/j.jmb.2004.07.060;
RA Haupt M., Bramkamp M., Coles M., Altendorf K., Kessler H.;
RT "Inter-domain motions of the N-domain of the KdpFABC complex, a P-type
RT ATPase, are not driven by ATP-induced conformational changes.";
RL J. Mol. Biol. 342:1547-1558(2004).
RN [16] {ECO:0007744|PDB:2A00, ECO:0007744|PDB:2A29}
RP STRUCTURE BY NMR OF 316-451 IN COMPLEX WITH ATP ANALOG, FUNCTION AS AN
RP ATPASE, ATP-BINDING, AND MUTAGENESIS OF PHE-377; SER-384; LYS-395 AND
RP ASP-399.
RX PubMed=16354672; DOI=10.1074/jbc.m508290200;
RA Haupt M., Bramkamp M., Heller M., Coles M., Deckers-Hebestreit G.,
RA Herkenhoff-Hesselmann B., Altendorf K., Kessler H.;
RT "The holo-form of the nucleotide binding domain of the KdpFABC complex from
RT Escherichia coli reveals a new binding mode.";
RL J. Biol. Chem. 281:9641-9649(2006).
RN [17] {ECO:0007744|PDB:5MRW}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 9-682 IN COMPLEX WITH KDPA; KDPC
RP AND KDPF, PHOSPHORYLATION AT SER-162, ACTIVITY REGULATION, SUBUNIT,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND DOMAIN.
RX PubMed=28636601; DOI=10.1038/nature22970;
RA Huang C.S., Pedersen B.P., Stokes D.L.;
RT "Crystal structure of the potassium-importing KdpFABC membrane complex.";
RL Nature 546:681-685(2017).
RN [18] {ECO:0007744|PDB:6HRA, ECO:0007744|PDB:6HRB}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF KDPFABC COMPLEX IN E1
RP AND E2 STATE, FUNCTION, REACTION MECHANISM, PHOSPHORYLATION AT SER-162,
RP ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=30478378; DOI=10.1038/s41467-018-07319-2;
RA Stock C., Hielkema L., Tascon I., Wunnicke D., Oostergetel G.T.,
RA Azkargorta M., Paulino C., Haenelt I.;
RT "Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two
RT inter-subunit half-channels.";
RL Nat. Commun. 9:4971-4971(2018).
RN [19] {ECO:0007744|PDB:7BGY, ECO:0007744|PDB:7BH1, ECO:0007744|PDB:7BH2, ECO:0007744|PDB:7LC3, ECO:0007744|PDB:7LC6}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF KDPFABC COMPLEX IN
RP MAJOR ENZYMATIC STATES, FUNCTION, REACTION MECHANISM, CATALYTIC ACTIVITY,
RP AND DOMAIN.
RX PubMed=34272288; DOI=10.1073/pnas.2105195118;
RA Sweet M.E., Larsen C., Zhang X., Schlame M., Pedersen B.P., Stokes D.L.;
RT "Structural basis for potassium transport in prokaryotes by KdpFABC.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
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
CC (PubMed:23930894, PubMed:2849541, PubMed:8499455). This subunit is
CC responsible for energy coupling to the transport system and for the
CC release of the potassium ions to the cytoplasm (PubMed:16354672,
CC PubMed:30478378, PubMed:34272288). {ECO:0000269|PubMed:16354672,
CC ECO:0000269|PubMed:23930894, ECO:0000269|PubMed:2849541,
CC ECO:0000269|PubMed:30478378, ECO:0000269|PubMed:34272288,
CC ECO:0000269|PubMed:8499455}.
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:0000255|HAMAP-
CC Rule:MF_00285, ECO:0000269|PubMed:2849541,
CC ECO:0000269|PubMed:34272288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16778;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00285,
CC ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:34272288};
CC -!- ACTIVITY REGULATION: ATPase activity is inhibited by phosphorylation at
CC Ser-162 (PubMed:28636601, PubMed:30478378). ATPase activity is
CC inhibited by vanadate, fluorescein isothiocyanate, N,N'-
CC dicyclohexylcarbodiimide and N-ethylmaleimide.
CC {ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:28636601,
CC ECO:0000269|PubMed:30478378}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC (PubMed:2849541, PubMed:9858692, PubMed:28636601,
CC PubMed:30478378). The complex also contains KdpF, a small non-essential
CC subunit (PubMed:10608856, PubMed:28636601, PubMed:30478378). The
CC KdpFABC complex exists as a dimer above concentrations of 30-50 nM,
CC whereas the complex exists as a functional monomer at lower
CC concentrations (PubMed:18298081). {ECO:0000269|PubMed:10608856,
CC ECO:0000269|PubMed:18298081, ECO:0000269|PubMed:2849541,
CC ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378,
CC ECO:0000269|PubMed:9858692}.
CC -!- INTERACTION:
CC P03960; P03961: kdpC; NbExp=2; IntAct=EBI-1116956, EBI-6997216;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00285, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2849541,
CC ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00285,
CC ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:28636601,
CC ECO:0000269|PubMed:30478378}.
CC -!- INDUCTION: Transcriptionally regulated by the KdpD/KdpE two-component
CC regulatory system. {ECO:0000269|PubMed:1532387}.
CC -!- DOMAIN: A protein-embedded tunnel connects the potassium ion in KdpA to
CC a water molecule at the canonical cation site in the transmembrane
CC domain of KdpB (PubMed:28636601, PubMed:30478378, PubMed:34272288). The
CC structures suggest a translocation pathway for potassium via two inter-
CC subunit half-channels along KdpA and KdpB, integrating KdpB directly in
CC the transport process (PubMed:30478378). The periplasmic potassium ion
CC probably enters the selectivity filter of KdpA, travels through the
CC water-filled tunnel to reach KdpB, and is released to the cytoplasm by
CC KdpB (PubMed:34272288). KdpB undergoes conformational changes, whereas
CC KdpA, KdpC and KdpF remain static (PubMed:34272288).
CC {ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378,
CC ECO:0000269|PubMed:34272288}.
CC -!- PTM: Phosphorylated at Ser-162, which leads to the inhibition of the
CC ATPase activity. {ECO:0000269|PubMed:28636601,
CC ECO:0000269|PubMed:30478378}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IA subfamily. {ECO:0000255|HAMAP-Rule:MF_00285}.
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DR EMBL; K02670; AAB96336.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73791.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35354.1; -; Genomic_DNA.
DR PIR; H64804; PWECBK.
DR RefSeq; NP_415225.1; NC_000913.3.
DR RefSeq; WP_000087939.1; NZ_SSZK01000045.1.
DR PDB; 1SVJ; NMR; -; A=316-451.
DR PDB; 1U7Q; NMR; -; A=316-451.
DR PDB; 2A00; NMR; -; A=316-451.
DR PDB; 2A29; NMR; -; A=316-451.
DR PDB; 5MRW; X-ray; 2.90 A; B/F/J=9-682.
DR PDB; 6HRA; EM; 3.70 A; B=1-682.
DR PDB; 6HRB; EM; 4.00 A; B=1-682.
DR PDB; 7BGY; EM; 2.90 A; B=1-682.
DR PDB; 7BH1; EM; 3.38 A; B=1-682.
DR PDB; 7BH2; EM; 3.00 A; B=1-682.
DR PDB; 7LC3; EM; 3.23 A; B=1-682.
DR PDB; 7LC6; EM; 3.70 A; B=1-682.
DR PDBsum; 1SVJ; -.
DR PDBsum; 1U7Q; -.
DR PDBsum; 2A00; -.
DR PDBsum; 2A29; -.
DR PDBsum; 5MRW; -.
DR PDBsum; 6HRA; -.
DR PDBsum; 6HRB; -.
DR PDBsum; 7BGY; -.
DR PDBsum; 7BH1; -.
DR PDBsum; 7BH2; -.
DR PDBsum; 7LC3; -.
DR PDBsum; 7LC6; -.
DR AlphaFoldDB; P03960; -.
DR SMR; P03960; -.
DR BioGRID; 4263067; 21.
DR ComplexPortal; CPX-3564; KdpFABC potassium import complex.
DR IntAct; P03960; 9.
DR MINT; P03960; -.
DR STRING; 511145.b0697; -.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR TCDB; 3.A.3.7.1; the p-type atpase (p-atpase) superfamily.
DR PaxDb; P03960; -.
DR PRIDE; P03960; -.
DR EnsemblBacteria; AAC73791; AAC73791; b0697.
DR EnsemblBacteria; BAA35354; BAA35354; BAA35354.
DR GeneID; 947450; -.
DR KEGG; ecj:JW0685; -.
DR KEGG; eco:b0697; -.
DR PATRIC; fig|1411691.4.peg.1578; -.
DR EchoBASE; EB0509; -.
DR eggNOG; COG2216; Bacteria.
DR InParanoid; P03960; -.
DR OMA; ILWLWFT; -.
DR PhylomeDB; P03960; -.
DR BioCyc; EcoCyc:KDPB-MON; -.
DR BioCyc; MetaCyc:KDPB-MON; -.
DR BRENDA; 7.2.2.6; 2026.
DR EvolutionaryTrace; P03960; -.
DR PRO; PR:P03960; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0031004; C:potassium ion-transporting ATPase complex; IDA:EcoCyc.
DR GO; GO:1903103; C:potassium:proton antiporter complex; IPI:ComplexPortal.
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; IDA:EcoCyc.
DR GO; GO:0098655; P:cation transmembrane transport; IDA:EcoCyc.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006813; P:potassium ion transport; IDA:ComplexPortal.
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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR43743; PTHR43743; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..682
FT /note="Potassium-transporting ATPase ATP-binding subunit"
FT /id="PRO_0000046115"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601"
FT TRANSMEM 34..55
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 56..61
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601"
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 81..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601"
FT TRANSMEM 223..242
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 243..251
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601"
FT TRANSMEM 252..263
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 264..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 596..612
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601"
FT TRANSMEM 613..631
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 632..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601"
FT TRANSMEM 654..678
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 679..682
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601"
FT ACT_SITE 307
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285,
FT ECO:0000269|PubMed:1474895"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285,
FT ECO:0000269|PubMed:16354672, ECO:0007744|PDB:2A00,
FT ECO:0007744|PDB:2A29"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285,
FT ECO:0000269|PubMed:16354672, ECO:0007744|PDB:2A00"
FT BINDING 377..384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285,
FT ECO:0000269|PubMed:16354672, ECO:0007744|PDB:2A00,
FT ECO:0007744|PDB:2A29"
FT BINDING 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285,
FT ECO:0000269|PubMed:16354672, ECO:0007744|PDB:2A00,
FT ECO:0007744|PDB:2A29"
FT BINDING 518
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 522
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000269|PubMed:30478378"
FT MUTAGEN 300
FT /note="D->E,N: Does not affect formation of the
FT phosphorylated intermediate."
FT /evidence="ECO:0000269|PubMed:1474895"
FT MUTAGEN 307
FT /note="D->E,N,Q: Unable to form a phosphorylated
FT intermediate and lacks ATPase activity."
FT /evidence="ECO:0000269|PubMed:1474895"
FT MUTAGEN 377
FT /note="F->A: Loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:16354672"
FT MUTAGEN 377
FT /note="F->Y: Slight decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:16354672"
FT MUTAGEN 384
FT /note="S->A,T: Decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:16354672"
FT MUTAGEN 395
FT /note="K->A: Strong decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:16354672"
FT MUTAGEN 399
FT /note="D->A: Decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:16354672"
FT CONFLICT 111..112
FT /note="EP -> DA (in Ref. 1; AAB96336)"
FT /evidence="ECO:0000305"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:7BGY"
FT HELIX 34..56
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 63..102
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 144..154
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:7BH2"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 216..237
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:7BGY"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:7BGY"
FT HELIX 330..341
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 347..360
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:7BH2"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 414..426
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 438..447
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 477..485
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 496..507
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 519..522
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 523..528
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 529..536
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 539..545
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 557..581
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 583..594
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 595..598
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 600..605
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 613..637
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 646..679
FT /evidence="ECO:0007829|PDB:5MRW"
SQ SEQUENCE 682 AA; 72199 MW; 4718AE78ECDA476C CRC64;
MSRKQLALFE PTLVVQALKE AVKKLNPQAQ WRNPVMFIVW IGSLLTTCIS IAMASGAMPG
NALFSAAISG WLWITVLFAN FAEALAEGRS KAQANSLKGV KKTAFARKLR EPKYGAAADK
VPADQLRKGD IVLVEAGDII PCDGEVIEGG ASVDESAITG ESAPVIRESG GDFASVTGGT
RILSDWLVIE CSVNPGETFL DRMIAMVEGA QRRKTPNEIA LTILLIALTI VFLLATATLW
PFSAWGGNAV SVTVLVALLV CLIPTTIGGL LSAIGVAGMS RMLGANVIAT SGRAVEAAGD
VDVLLLDKTG TITLGNRQAS EFIPAQGVDE KTLADAAQLA SLADETPEGR SIVILAKQRF
NLRERDVQSL HATFVPFTAQ SRMSGINIDN RMIRKGSVDA IRRHVEANGG HFPTDVDQKV
DQVARQGATP LVVVEGSRVL GVIALKDIVK GGIKERFAQL RKMGIKTVMI TGDNRLTAAA
IAAEAGVDDF LAEATPEAKL ALIRQYQAEG RLVAMTGDGT NDAPALAQAD VAVAMNSGTQ
AAKEAGNMVD LDSNPTKLIE VVHIGKQMLM TRGSLTTFSI ANDVAKYFAI IPAAFAATYP
QLNALNIMCL HSPDSAILSA VIFNALIIVF LIPLALKGVS YKPLTASAML RRNLWIYGLG
GLLVPFIGIK VIDLLLTVCG LV
