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HPRK_XANCP
ID   HPRK_XANCP              Reviewed;         316 AA.
AC   Q8P709;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=HPr kinase/phosphorylase {ECO:0000255|HAMAP-Rule:MF_01249};
DE            Short=HPrK/P {ECO:0000255|HAMAP-Rule:MF_01249};
DE            EC=2.7.11.- {ECO:0000255|HAMAP-Rule:MF_01249};
DE            EC=2.7.4.- {ECO:0000255|HAMAP-Rule:MF_01249};
DE   AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000255|HAMAP-Rule:MF_01249};
GN   Name=hprK {ECO:0000255|HAMAP-Rule:MF_01249}; Synonyms=ptsK;
GN   OrderedLocusNames=XCC2805;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent
CC       phosphorylation of a specific serine residue in HPr, a phosphocarrier
CC       protein of the phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS). HprK/P also catalyzes the pyrophosphate-producing,
CC       inorganic phosphate-dependent dephosphorylation (phosphorolysis) of
CC       seryl-phosphorylated HPr (P-Ser-HPr). {ECO:0000255|HAMAP-
CC       Rule:MF_01249}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-
CC         serine + ADP + H(+); Xref=Rhea:RHEA:46600, Rhea:RHEA-COMP:11602,
CC         Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[HPr protein]-O-phospho-L-serine + H(+) + phosphate = [HPr
CC         protein]-L-serine + diphosphate; Xref=Rhea:RHEA:46604, Rhea:RHEA-
CC         COMP:11602, Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
CC       {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried out
CC       by the same active site and suggest a common mechanism for both
CC       reactions. {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000255|HAMAP-
CC       Rule:MF_01249}.
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DR   EMBL; AE008922; AAM42077.1; -; Genomic_DNA.
DR   RefSeq; NP_638153.1; NC_003902.1.
DR   RefSeq; WP_005993219.1; NC_003902.1.
DR   AlphaFoldDB; Q8P709; -.
DR   SMR; Q8P709; -.
DR   STRING; 340.xcc-b100_1355; -.
DR   EnsemblBacteria; AAM42077; AAM42077; XCC2805.
DR   GeneID; 58012595; -.
DR   KEGG; xcc:XCC2805; -.
DR   PATRIC; fig|190485.4.peg.2993; -.
DR   eggNOG; COG1493; Bacteria.
DR   HOGENOM; CLU_052030_0_2_6; -.
DR   OMA; AMNNRQK; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01918; HprK_C; 1.
DR   Gene3D; 3.40.1390.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01249; HPr_kinase; 1.
DR   InterPro; IPR003755; HPr(Ser)_kin/Pase.
DR   InterPro; IPR011104; Hpr_kin/Pase_C.
DR   InterPro; IPR011126; Hpr_kin/Pase_Hpr_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR   PANTHER; PTHR30305:SF1; PTHR30305:SF1; 1.
DR   Pfam; PF07475; Hpr_kinase_C; 1.
DR   Pfam; PF02603; Hpr_kinase_N; 1.
DR   SUPFAM; SSF75138; SSF75138; 1.
DR   TIGRFAMs; TIGR00679; hpr-ser; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Multifunctional enzyme;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..316
FT                   /note="HPr kinase/phosphorylase"
FT                   /id="PRO_0000059007"
FT   REGION          206..215
FT                   /note="Important for the catalytic mechanism of both
FT                   phosphorylation and dephosphorylation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   REGION          272..277
FT                   /note="Important for the catalytic mechanism of
FT                   dephosphorylation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        182
FT                   /note="Proton acceptor; for phosphorylation activity.
FT                   Proton donor; for dephosphorylation activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        251
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         158..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         207
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
SQ   SEQUENCE   316 AA;  35154 MW;  7E871C4DD0E9ADEF CRC64;
     MNTSITAREL FDQQRDKLAL RWVAGQKGEH REIQAGSNNA RRPSLAGYLN VIYPNKVQIL
     GTEELAWLDS LDARQRWETI EKIIQVQPLA LAISKNQSCP EDLRAAADES NTPLWISPKR
     GHELLNHLSY HLARTLAPRV TLHGVFMEIY SIGVLITGEA GSGKSELALE LLSRGHRLVA
     DDAPEFTQIA PDVLDGTCPE LLQDLLEVRG LGVLNVRDMF GDTAVKKNKY LRLIVHLTRP
     MTEPTPSGYE RLTGDSGSRH VLDLDVPLIT LPVMPGRNLA VLTEAATRLH ILRTKGIDPA
     AMFIARHSNL LERRTP
 
 
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