HPRK_BACAC
ID HPRK_BACAC Reviewed; 309 AA.
AC C3LED2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=BAMEG_5445;
OS Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=568206;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 684 / NRRL 3495;
RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA Sutton G., Sims D.;
RT "Genome sequence of Bacillus anthracis str. CDC 684.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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). The two antagonistic activities
CC of HprK/P are regulated by several intracellular metabolites, which
CC change their concentration in response to the absence or presence of
CC rapidly metabolisable carbon sources (glucose, fructose, etc.) in the
CC growth medium. Also phosphorylates/dephosphorylates the HPr-like
CC catabolite repression protein crh on a specific serine residue.
CC Therefore, by controlling the phosphorylation state of HPr and crh,
CC HPrK/P is a sensor enzyme that plays a major role in the regulation of
CC carbon metabolism and sugar transport: it mediates carbon catabolite
CC repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and
CC inducer exclusion. {ECO:0000255|HAMAP-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; CP001215; ACP14549.1; -; Genomic_DNA.
DR RefSeq; WP_001127244.1; NC_012581.1.
DR AlphaFoldDB; C3LED2; -.
DR SMR; C3LED2; -.
DR GeneID; 45024995; -.
DR GeneID; 64200814; -.
DR KEGG; bah:BAMEG_5445; -.
DR HOGENOM; CLU_052030_0_1_9; -.
DR OMA; AMNNRQK; -.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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; Carbohydrate metabolism; Kinase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..309
FT /note="HPr kinase/phosphorylase"
FT /id="PRO_1000165067"
FT REGION 201..210
FT /note="Important for the catalytic mechanism of both
FT phosphorylation and dephosphorylation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT REGION 264..269
FT /note="Important for the catalytic mechanism of
FT dephosphorylation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT ACT_SITE 159
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT ACT_SITE 177
FT /note="Proton acceptor; for phosphorylation activity.
FT Proton donor; for dephosphorylation activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
SQ SEQUENCE 309 AA; 34587 MW; 4CF32C76AC8BE6E7 CRC64;
MPKVRTKDLI EQFQLELISG EEGIHRPIDT SDLSRPGIEM AGFFTYYPAD RVQLLGKTEL
TFFDTLTSDQ KQERMKALCT EETPCIIVTR NQDVPDELLQ ASRESGMPLL RSSQTTTRLS
SRLTNYLEGK LAPTTAVHGV LVDIYGVGVL ITGQSGVGKS ETALELVKRG HRLVADDSVE
IRQEDEDMLV GSSPDLIEHL LEIRGLGIIN VMTLFGAGAV RNYKRITLVI NLEIWDQKKN
YDRLGLDEEK MKIIDTELTK ITLPVRPGRN LAVIIEVAAM NFRLKRMGVN AAQQFSERLM
SAIELGNQE
