ID R9LZB7_9FIRM Unreviewed; 317 AA.
AC R9LZB7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=C814_00580 {ECO:0000313|EMBL:EOS64150.1};
OS Anaerotruncus sp. G3(2012).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=1235835 {ECO:0000313|EMBL:EOS64150.1, ECO:0000313|Proteomes:UP000014129};
RN [1] {ECO:0000313|EMBL:EOS64150.1, ECO:0000313|Proteomes:UP000014129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G3(2012) {ECO:0000313|Proteomes:UP000014129};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anaerotruncus bacterium G3.";
RL Submitted (APR-2013) 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. Therefore, by controlling the phosphorylation state of
CC HPr, HPrK/P is a sensor enzyme that plays a major role in the
CC regulation of carbon metabolism and sugar transport: it mediates carbon
CC catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate
CC uptake and 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:EOS64150.1}.
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DR EMBL; ASTA01000014; EOS64150.1; -; Genomic_DNA.
DR RefSeq; WP_016315288.1; NZ_KE159657.1.
DR AlphaFoldDB; R9LZB7; -.
DR STRING; 1235835.C814_00580; -.
DR PATRIC; fig|1235835.3.peg.615; -.
DR eggNOG; COG1493; Bacteria.
DR HOGENOM; CLU_052030_0_1_9; -.
DR OrthoDB; 9778803at2; -.
DR Proteomes; UP000014129; 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}; Carbohydrate metabolism {ECO:0000256|HAMAP-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:UP000014129};
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 7..129
FT /note="HPr(Ser) kinase/phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02603"
FT DOMAIN 134..302
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 268..273
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 247
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; 35344 MW; D4F772D35B07A2DD CRC64;
MATKFIVPLQ KLIKIFNLEV LYLPKEAGDI SISSPEIDRP GLPLSGFFDY FDNQRIQIMG
KSELAFLEQF DEAERARRID NYFANKPPAV VITRNLDFPP RIRDAAEKNE VALLRTSEGT
SSFLAALIAE LNVELAPRVT RHGVLVEVYG EGILLMGESG VGKSEAAIEL VKRGHRLIAD
DAVELRRVSN KSIVGSSPEN IRHFMELRGV GIINARRLFG IGAVKMTEKI NMLVQLEQWD
ASKVYDRMGM NDEYTDVLGI QIPSLTIPVK PGRNIAIIIE VAAMNNRQKR MGYNAAQELL
EKLGMVEPDG GSDWSSF
//
