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HPRK_METPP
ID   HPRK_METPP              Reviewed;         318 AA.
AC   A2SC97;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=Mpe_A0224;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM93186.1; -; Genomic_DNA.
DR   RefSeq; WP_011827825.1; NC_008825.1.
DR   AlphaFoldDB; A2SC97; -.
DR   SMR; A2SC97; -.
DR   STRING; 420662.Mpe_A0224; -.
DR   EnsemblBacteria; ABM93186; ABM93186; Mpe_A0224.
DR   KEGG; mpt:Mpe_A0224; -.
DR   eggNOG; COG1493; Bacteria.
DR   HOGENOM; CLU_052030_0_2_4; -.
DR   OMA; AMNNRQK; -.
DR   OrthoDB; 391150at2; -.
DR   Proteomes; UP000000366; Chromosome.
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..318
FT                   /note="HPr kinase/phosphorylase"
FT                   /id="PRO_1000067160"
FT   REGION          209..218
FT                   /note="Important for the catalytic mechanism of both
FT                   phosphorylation and dephosphorylation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   REGION          273..278
FT                   /note="Important for the catalytic mechanism of
FT                   dephosphorylation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        185
FT                   /note="Proton acceptor; for phosphorylation activity.
FT                   Proton donor; for dephosphorylation activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         161..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         210
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
SQ   SEQUENCE   318 AA;  35815 MW;  A3674C22EDBD0BB4 CRC64;
     MKPTVISAEA LFEAHRTALR WEWLAGHAHP ERRFDEVAVR DAQSAADLVG YLNYIHPYRV
     QIVGRREVRY LVDVPPEDQE RRISRIVTLE PPVVIVADQQ TPPDRLVAMC ERADIPLFVT
     EESAGHVIDV LRAHLSQHFA DRTTRHGVFM DILGLGVLLT GESGLGKSEL GLELISRGHG
     LVADDAVDLY RVSQTALEGR CPDLLLNLLE VRGIGLLDIK AIFGETAVRR KMRLKLIVHL
     VRKETMERDF ERLPYEPLYE DVLDVPVLKA VIAVDAGRNL AVLVEAAVRN TILKLRGIDT
     YQEFIARHRI AMEGDEPI
 
 
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