ID A0A4R2IC93_9GAMM Unreviewed; 317 AA.
AC A0A4R2IC93;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=EV148_102522 {ECO:0000313|EMBL:TCO42163.1};
OS Dokdonella fugitiva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=328517 {ECO:0000313|EMBL:TCO42163.1, ECO:0000313|Proteomes:UP000294862};
RN [1] {ECO:0000313|EMBL:TCO42163.1, ECO:0000313|Proteomes:UP000294862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3 {ECO:0000313|EMBL:TCO42163.1,
RC ECO:0000313|Proteomes:UP000294862};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
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:0000256|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: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:TCO42163.1}.
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DR EMBL; SLWQ01000002; TCO42163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R2IC93; -.
DR OrthoDB; 9778803at2; -.
DR Proteomes; UP000294862; 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: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 InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
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.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, 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}; Reference proteome {ECO:0000313|Proteomes:UP000294862};
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 6..129
FT /note="HPr(Ser) kinase/phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02603"
FT DOMAIN 134..306
FT /note="HPr kinase/phosphorylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07475"
FT REGION 205..214
FT /note="Important for the catalytic mechanism of both
FT phosphorylation and dephosphorylation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT REGION 272..277
FT /note="Important for the catalytic mechanism of
FT dephosphorylation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 142
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 163
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 181
FT /note="Proton acceptor; for phosphorylation activity.
FT Proton donor; for dephosphorylation activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 251
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
SQ SEQUENCE 317 AA; 35517 MW; C8705BA34703750F CRC64;
MDRLTARQLF DAVSERLSLR WAAGLRGEQR AIDTGDTLER RPSLVGYLNI IYPNKVQIVG
TEELKYLDGL DSRQRWETVE KIMAYQPTAL LVSKDQAVPA DLRQAAEESN TPLWISPKRG
HELLTYLQYQ LARTLARQVT LHGVLMEVYS IGVLITGESG TGKSELALEL LTRGHRLVAD
DAPEFTLIAP DVIDGTCPEM LRDLLEVRGL GVLNVREMFG HTAVKPSKYL RLIVHLKPQK
LDVPHGDAMT RLTGDVGYRE VLDVHVPQIT IPVAPGRNIA VLAEAAVRSH MLKSKGFDPA
QTFIDRQAHQ MRRLPPW
//
