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HPr kinase/phosphorylase (HPrK/P) (EC 2.7.11.-) (EC 2.7.4.-) (HPr(Ser) kinase/phosphorylase)

 A0A0A3JUY2_9BACI        Unreviewed;       312 AA.
A0A0A3JUY2;
04-FEB-2015, integrated into UniProtKB/TrEMBL.
04-FEB-2015, sequence version 1.
10-APR-2019, entry version 27.
RecName: Full=HPr kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00754002};
Short=HPrK/P {ECO:0000256|HAMAP-Rule:MF_01249};
EC=2.7.11.- {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00754007};
EC=2.7.4.- {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00754021};
AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249};
Name=hprK {ECO:0000256|HAMAP-Rule:MF_01249};
ORFNames=CD30_09575 {ECO:0000313|EMBL:KGR90777.1};
Lysinibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
Lysinibacillus.
NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR90777.1, ECO:0000313|Proteomes:UP000030595};
[1] {ECO:0000313|EMBL:KGR90777.1, ECO:0000313|Proteomes:UP000030595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR90777.1,
ECO:0000313|Proteomes:UP000030595};
Zhang F., Wang G., Zhang L.;
"Draft genome sequence of Lysinibacillus massiliensis CCUG 49529.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-
dependent phosphorylation of a specific serine residue in HPr, a
phosphocarrier protein of the phosphoenolpyruvate-dependent sugar
phosphotransferase system (PTS). HprK/P also catalyzes the
pyrophosphate-producing, inorganic phosphate-dependent
dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-
Ser-HPr). The two antagonistic activities of HprK/P are regulated
by several intracellular metabolites, which change their
concentration in response to the absence or presence of rapidly
metabolisable carbon sources (glucose, fructose, etc.) in the
growth medium. Also phosphorylates/dephosphorylates the HPr-like
catabolite repression protein crh on a specific serine residue.
Therefore, by controlling the phosphorylation state of HPr and
crh, HPrK/P is a sensor enzyme that plays a major role in the
regulation of carbon metabolism and sugar transport: it mediates
carbon catabolite repression (CCR), and regulates PTS-catalyzed
carbohydrate uptake and inducer exclusion. {ECO:0000256|HAMAP-
Rule:MF_01249}.
-!- CATALYTIC ACTIVITY:
Reaction=[HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-
serine + ADP + H(+); Xref=Rhea:RHEA:46600, Rhea:RHEA-COMP:11602,
Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
Evidence={ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS01117191};
-!- CATALYTIC ACTIVITY:
Reaction=[HPr protein]-O-phospho-L-serine + H(+) + phosphate =
[HPr protein]-L-serine + diphosphate; Xref=Rhea:RHEA:46604,
Rhea:RHEA-COMP:11602, Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
ChEBI:CHEBI:83421; Evidence={ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS01117182};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754019};
-!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754027}.
-!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
{ECO:0000256|HAMAP-Rule:MF_01249}.
-!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried
out by the same active site and suggest a common mechanism for
both reactions. {ECO:0000256|HAMAP-Rule:MF_01249}.
-!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000256|HAMAP-
Rule:MF_01249, ECO:0000256|SAAS:SAAS00754005}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KGR90777.1}.
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EMBL; JPVQ01000014; KGR90777.1; -; Genomic_DNA.
RefSeq; WP_036175738.1; NZ_JPVQ01000014.1.
STRING; 1211035.CD30_09575; -.
EnsemblBacteria; KGR90777; KGR90777; CD30_09575.
OrthoDB; 391150at2; -.
Proteomes; UP000030595; Unassembled WGS sequence.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
CDD; cd01918; HprK_C; 1.
Gene3D; 3.40.1390.20; -; 1.
HAMAP; MF_01249; HPr_kinase; 1.
InterPro; IPR003755; HPr(Ser)_kin/Pase.
InterPro; IPR011104; Hpr_kin/Pase_C.
InterPro; IPR011126; Hpr_kin/Pase_Hpr_N.
InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
PANTHER; PTHR30305:SF1; PTHR30305:SF1; 1.
Pfam; PF07475; Hpr_kinase_C; 1.
Pfam; PF02603; Hpr_kinase_N; 1.
SUPFAM; SSF75138; SSF75138; 1.
TIGRFAMs; TIGR00679; hpr-ser; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754014};
Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01249};
Complete proteome {ECO:0000313|Proteomes:UP000030595};
Kinase {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754023};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754024};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754029};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754025};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754014};
Reference proteome {ECO:0000313|Proteomes:UP000030595};
Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754023};
Transferase {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754023}.
DOMAIN 4 127 Hpr_kinase_N. {ECO:0000259|Pfam:PF02603}.
DOMAIN 130 298 Hpr_kinase_C. {ECO:0000259|Pfam:PF07475}.
NP_BIND 153 160 ATP. {ECO:0000256|HAMAP-Rule:MF_01249}.
REGION 201 210 Important for the catalytic mechanism of
both phosphorylation and
dephosphorylation. {ECO:0000256|HAMAP-
Rule:MF_01249}.
REGION 264 269 Important for the catalytic mechanism of
dephosphorylation. {ECO:0000256|HAMAP-
Rule:MF_01249}.
ACT_SITE 138 138 {ECO:0000256|HAMAP-Rule:MF_01249}.
ACT_SITE 159 159 {ECO:0000256|HAMAP-Rule:MF_01249}.
ACT_SITE 177 177 Proton acceptor; for phosphorylation
activity. Proton donor; for
dephosphorylation activity.
{ECO:0000256|HAMAP-Rule:MF_01249}.
ACT_SITE 243 243 {ECO:0000256|HAMAP-Rule:MF_01249}.
METAL 160 160 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01249}.
METAL 202 202 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01249}.
SEQUENCE 312 AA; 34777 MW; 40A76F24322A794D CRC64;
MIQVTSKDVM EKFNLNLVSG NEGIGRYITT SDISRPGLEM AGYFTHYPAN RVQLIGRTEL
SFFDMLPSNL KYERMLKLCS QDTPAIIISR GMEVPEELIQ ASNENSVPVL TTSMKTTRFS
SRLTNFLESK LAPSAAMHGV LVDVYGIGVL IIGKSGVGKS ETALELIKKG HRLVADDCVE
IRQEAEDLIV GSPPPLLEHL LEIRGIGIID IITLFGASAV RPKKRITLIV ELENWDPEKV
YDRLGLDEEK MKIIDTEITK LTIPVQPGRN VSVIIEVAAM NYRLKKLGVN AAQEFSRRLD
EVISMQDDLD DY


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