ID A0A544TR93_9BACI Unreviewed; 311 AA.
AC A0A544TR93;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=HPr kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249};
DE Short=HPrK/P {ECO:0000256|HAMAP-Rule:MF_01249};
DE EC=2.7.11.- {ECO:0000256|HAMAP-Rule:MF_01249};
DE EC=2.7.4.- {ECO:0000256|HAMAP-Rule:MF_01249};
DE AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249};
GN Name=hprK {ECO:0000256|HAMAP-Rule:MF_01249};
GN ORFNames=FG384_09970 {ECO:0000313|EMBL:TQR19977.1};
OS Psychrobacillus vulpis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=2325572 {ECO:0000313|EMBL:TQR19977.1, ECO:0000313|Proteomes:UP000316626};
RN [1] {ECO:0000313|EMBL:TQR19977.1, ECO:0000313|Proteomes:UP000316626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z8 {ECO:0000313|EMBL:TQR19977.1,
RC ECO:0000313|Proteomes:UP000316626};
RA Rodriguez M., Reina J.C., Bejar V., Llamas I.;
RT "Psychrobacillus vulpis sp. nov., a new species isolated from feces of a
RT red fox that inhabits in The Tablas de Daimiel Natural Park, Albacete,
RT Spain.";
RL Submitted (JUN-2019) 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:0000256|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:0000256|ARBA:ARBA00001120, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00001319,
CC ECO:0000256|HAMAP-Rule:MF_01249};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01249};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01249}.
CC -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01249}.
CC -!- SIMILARITY: Belongs to the HPrK/P family.
CC {ECO:0000256|ARBA:ARBA00006883, ECO:0000256|HAMAP-Rule:MF_01249}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TQR19977.1}.
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DR EMBL; VDGI01000009; TQR19977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A544TR93; -.
DR OrthoDB; 9778803at2; -.
DR Proteomes; UP000316626; Unassembled WGS sequence.
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; HprK N-terminal domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00679; hpr-ser; 1.
DR PANTHER; PTHR30305:SF1; HPR KINASE_PHOSPHORYLASE; 1.
DR PANTHER; PTHR30305; UNCHARACTERIZED; 1.
DR Pfam; PF07475; Hpr_kinase_C; 1.
DR Pfam; PF02603; Hpr_kinase_N; 1.
DR SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01249};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01249};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01249};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01249};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01249};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01249};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01249};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|HAMAP-Rule:MF_01249};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01249}.
FT DOMAIN 4..127
FT /note="HPr(Ser) kinase/phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02603"
FT DOMAIN 130..298
FT /note="HPr kinase/phosphorylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07475"
FT REGION 201..210
FT /note="Important for the catalytic mechanism of both
FT phosphorylation and dephosphorylation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT REGION 264..269
FT /note="Important for the catalytic mechanism of
FT dephosphorylation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 159
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 177
FT /note="Proton acceptor; for phosphorylation activity.
FT Proton donor; for dephosphorylation activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 243
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
SQ SEQUENCE 311 AA; 34429 MW; 9CB0E1645D7A817D CRC64;
MPHVTTKDVK EKFNLTLVSG EEGIGRHIAI SDISRPGIEI AGYFTHYPSN RIQLLGKTEI
SFFQLLETSE KIERALKLCE ADTPAIIISH DMEVPQELID ASNEKSVPVL TTKMPTTRFS
SLLTNFLESK LAPTTAVHGV LVDIYGVGIL ITGKSGVGKS ETALELVKRG HRLVADDCVE
IRQEGEDTLV GNAPKLIEHL LEIRGLGIID IMTLFGASAI RSYKRITLVI ELEIWDAEKT
YDRLGLEEEK MEIINTAITK LTVPVRPGRN LAVIIEVAAM NHRLKRMGVN AAEDFAKRLD
DVISQNGESE Y
//
