HPRK_LEPBJ
ID HPRK_LEPBJ Reviewed; 318 AA.
AC Q04SV2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, 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=LBJ_1445;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000350; ABJ76018.1; -; Genomic_DNA.
DR RefSeq; WP_011671756.1; NC_008510.1.
DR AlphaFoldDB; Q04SV2; -.
DR SMR; Q04SV2; -.
DR EnsemblBacteria; ABJ76018; ABJ76018; LBJ_1445.
DR KEGG; lbj:LBJ_1445; -.
DR HOGENOM; CLU_052030_0_1_12; -.
DR OMA; AMNNRQK; -.
DR Proteomes; UP000000656; Chromosome 1.
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; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..318
FT /note="HPr kinase/phosphorylase"
FT /id="PRO_1000067157"
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 269..274
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 248
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 318 AA; 35791 MW; 3617FFC56EBCD626 CRC64;
MSMPGINVSN LLNEHEELGL RLLAGEKGLT NRINMSEINR PGLSLTGFYE SFAHDRIQIF
GKGEWAYITS RIPEDLKNIA ADFFSFHLNC IIFTHGNMPP PIFTENCERL AIPLMISDVS
THKFITLISG ILDRSLAPRT MRHGVLIEVF GIGILLSGKS GVGKSETALE LIERGHRLVA
DDMVEIRRLS ESYLIGTCSD LLRHHMEIRG LGILNIKDIF GIGSVRDHKL IELIIRLEEW
TEDKDFDRTG LENPTEELLG VQIPLIRVPV KPGRNIPIIV ETAAMNQRLR KLGKNAAQEF
NQKLSNYLQQ GKVERNPP
