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

 HPRK_BACSU              Reviewed;         310 AA.
O34483; Q9R9E3;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
07-JUN-2017, entry version 138.
RecName: Full=HPr kinase/phosphorylase;
Short=HPrK/P;
EC=2.7.11.-;
EC=2.7.4.-;
AltName: Full=HPr kinase/phosphatase;
AltName: Full=HPr(Ser) kinase/phosphorylase;
Name=hprK; Synonyms=ptsK, yvoB; OrderedLocusNames=BSU35000;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C.,
Karamata D.;
"Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
subtilis.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-310.
STRAIN=168;
Dartois V.A., Hoch J.A.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[4]
PHOSPHORYLATION OF CRH PROTEIN.
STRAIN=QB5081;
PubMed=9237995; DOI=10.1073/pnas.94.16.8439;
Galinier A., Haiech J., Kilhoffer M.-C., Jaquinod M., Stuelke J.,
Deutscher J., Martin-Verstraete I.;
"The Bacillus subtilis crh gene encodes a HPr-like protein involved in
carbon catabolite repression.";
Proc. Natl. Acad. Sci. U.S.A. 94:8439-8444(1997).
[5]
PROTEIN SEQUENCE OF 2-18, CHARACTERIZATION, AND MASS SPECTROMETRY.
PubMed=9570401; DOI=10.1046/j.1365-2958.1998.00747.x;
Reizer J., Hoischen C., Titgemeyer F., Rivolta C., Rabus R.,
Stuelke J., Karamata D., Saier M.H. Jr., Hillen W.;
"A novel protein kinase that controls carbon catabolite repression in
bacteria.";
Mol. Microbiol. 27:1157-1169(1998).
[6]
CHARACTERIZATION OF THE KINASE ACTIVITY.
PubMed=9465101; DOI=10.1073/pnas.95.4.1823;
Galinier A., Kravanja M., Engelmann R., Hengstenberg W.,
Kilhoffer M.-C., Deutscher J., Haiech J.;
"New protein kinase and protein phosphatase families mediate signal
transduction in bacterial catabolite repression.";
Proc. Natl. Acad. Sci. U.S.A. 95:1823-1828(1998).
[7]
FUNCTION.
PubMed=9987110; DOI=10.1046/j.1365-2958.1999.01146.x;
Kravanja M., Engelmann R., Dossonnet V., Bluggel M., Meyer H.E.,
Frank R., Galinier A., Deutscher J., Schnell N., Hengstenberg W.;
"The hprK gene of Enterococcus faecalis encodes a novel bifunctional
enzyme: the HPr kinase/phosphatase.";
Mol. Microbiol. 31:59-66(1999).
[8]
CHARACTERIZATION, AND COFACTOR.
PubMed=12009882; DOI=10.1021/bi025613y;
Lavergne J.-P., Jault J.-M., Galinier A.;
"Insights into the functioning of Bacillus subtilis HPr
kinase/phosphatase: affinity for its protein substrates and role of
cations and phosphate.";
Biochemistry 41:6218-6225(2002).
[9]
INDUCTION, AND MUTAGENESIS OF GLY-148.
PubMed=12055300;
Hanson K.G., Steinhauer K., Reizer J., Hillen W., Stuelke J.;
"HPr kinase/phosphatase of Bacillus subtilis: expression of the gene
and effects of mutations on enzyme activity, growth and carbon
catabolite repression.";
Microbiology 148:1805-1811(2002).
[10]
DEPHOSPHORYLATION REACTION MECHANISM.
PubMed=12359880; DOI=10.1073/pnas.212410399;
Mijakovic I., Poncet S., Galinier A., Monedero V., Fieulaine S.,
Janin J., Nessler S., Marquez J.A., Scheffzek K., Hasenbein S.,
Hengstenberg W., Deutscher J.;
"Pyrophosphate-producing protein dephosphorylation by HPr
kinase/phosphorylase: a relic of early life?";
Proc. Natl. Acad. Sci. U.S.A. 99:13442-13447(2002).
[11]
CHARACTERIZATION.
PubMed=12411438; DOI=10.1074/jbc.M209052200;
Ramstroem H., Sanglier S., Leize-Wagner E., Philippe C.,
van Dorsselaer A., Haiech J.;
"Properties and regulation of the bifunctional enzyme HPr
kinase/phosphatase in Bacillus subtilis.";
J. Biol. Chem. 278:1174-1185(2003).
[12]
MUTAGENESIS OF HIS-138; GLY-153; SER-155; GLY-156; GLY-158; LYS-159;
SER-160 AND HIS-171.
PubMed=12779331; DOI=10.1021/bi034405i;
Pompeo F., Granet Y., Lavergne J.-P., Grangeasse C., Nessler S.,
Jault J.-M., Galinier A.;
"Regulation and mutational analysis of the HPr kinase/phosphorylase
from Bacillus subtilis.";
Biochemistry 42:6762-6771(2003).
[13]
REVIEW.
PubMed=15023355; DOI=10.1016/j.bbapap.2003.11.018;
Poncet S., Mijakovic I., Nessler S., Gueguen-Chaignon V., Chaptal V.,
Galinier A., Boel G., Maze A., Deutscher J.;
"HPr kinase/phosphorylase, a Walker motif A-containing bifunctional
sensor enzyme controlling catabolite repression in Gram-positive
bacteria.";
Biochim. Biophys. Acta 1697:123-135(2004).
-!- FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-
dependent phosphorylation of 'Ser-45' 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 'Ser-46'. 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:0000269|PubMed:9987110}.
-!- CATALYTIC ACTIVITY: ATP + HPr = ADP + P-Ser-HPr.
-!- CATALYTIC ACTIVITY: P-Ser-HPr + phosphate = HPr + diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12009882};
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:12009882};
Note=The enzyme may harbor two different cation-binding sites, one
that interacts specifically with the nucleotide, and the other
that is involved in the binding of the protein substrate.
{ECO:0000269|PubMed:12009882};
-!- ENZYME REGULATION: Is active as a kinase only at high ATP
concentrations or at low ATP concentrations in the presence of the
allosteric activator fructose 1,6-bisphosphate (FBP). The
pyrophosphate-dependent HPr phosphorylation is not stimulated by
FBP. Kinase activity is inhibited by inorganic phosphate (Pi).
Dephosphorylation of HPr(Ser-P) by B.subtilis HPrK/P becomes
prevalent when the concentration of Pi increases. Thus, the kinase
activity may prevail under conditions of good nutrient supply,
whereas the phosphorylase activity is dominant if carbon and
energy sources become limiting.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=78 uM for HPr;
KM=85 uM for P-Ser-HPr;
KM=265 uM for phosphate;
KM=785 uM for pyrophosphate;
-!- SUBUNIT: Homohexamer.
-!- INTERACTION:
P11065:hpr; NbExp=3; IntAct=EBI-5242785, EBI-2121844;
O31435:ybdM; NbExp=5; IntAct=EBI-5242785, EBI-5255200;
P96716:ywqD; NbExp=2; IntAct=EBI-5242785, EBI-9302929;
-!- INDUCTION: Constitutively expressed, with or without glucose in
the growth medium. {ECO:0000269|PubMed:12055300}.
-!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
-!- MASS SPECTROMETRY: Mass=34529; Method=MALDI; Range=2-310;
Evidence={ECO:0000269|PubMed:9570401};
-!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried
out by the same active site and suggest a common mechanism for
both reactions.
-!- MISCELLANEOUS: According to PubMed:12779331, the mutation G152A
reduces the kinase activity about twofold and has little effect on
phosphorylase activity, whereas according to PubMed:12055300, it
completely prevents both functions. This conflicting result may be
explained by limiting amounts substrates conditions used in
PubMed:12779331 assays.
-!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000305}.
-!- CAUTION: Was originally called HPr kinase/phosphatase, but P-Ser-
HPr dephosphorylation was found to follow a quite unique mechanism
(PubMed:12359880), in which Pi instead of H(2)O is used for the
nucleophilic attack on the phosphoryl group. P-Ser-HPr
dephosphorylation is therefore not a phosphohydrolysis but a
phosphophosphorolysis reaction, and the bifunctional enzyme was
dubbed HPr kinase/phosphorylase. {ECO:0000305|PubMed:12359880}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF017113; AAC67286.1; -; Genomic_DNA.
EMBL; AL009126; CAB15505.1; -; Genomic_DNA.
EMBL; U63310; AAD09500.1; -; Genomic_DNA.
PIR; E70044; E70044.
RefSeq; NP_391380.1; NC_000964.3.
RefSeq; WP_003228097.1; NZ_JNCM01000033.1.
ProteinModelPortal; O34483; -.
SMR; O34483; -.
IntAct; O34483; 6.
STRING; 224308.Bsubs1_010100018946; -.
BindingDB; O34483; -.
ChEMBL; CHEMBL4974; -.
PaxDb; O34483; -.
EnsemblBacteria; CAB15505; CAB15505; BSU35000.
GeneID; 936615; -.
KEGG; bsu:BSU35000; -.
PATRIC; fig|224308.179.peg.3788; -.
eggNOG; ENOG4105D1C; Bacteria.
eggNOG; COG1493; LUCA.
HOGENOM; HOG000099173; -.
InParanoid; O34483; -.
KO; K06023; -.
OMA; IQKPGLA; -.
PhylomeDB; O34483; -.
BioCyc; BSUB:BSU35000-MONOMER; -.
SABIO-RK; O34483; -.
PRO; PR:O34483; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:InterPro.
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_N-like.
PANTHER; PTHR30305:SF5; PTHR30305:SF5; 1.
Pfam; PF07475; Hpr_kinase_C; 1.
Pfam; PF02603; Hpr_kinase_N; 1.
SUPFAM; SSF75138; SSF75138; 1.
TIGRFAMs; TIGR00679; hpr-ser; 1.
1: Evidence at protein level;
Allosteric enzyme; ATP-binding; Carbohydrate metabolism;
Complete proteome; Direct protein sequencing; Kinase; Magnesium;
Metal-binding; Multifunctional enzyme; Nucleotide-binding;
Reference proteome; Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9570401}.
CHAIN 2 310 HPr kinase/phosphorylase.
/FTId=PRO_0000058946.
NP_BIND 153 160 ATP. {ECO:0000305}.
REGION 201 210 Important for the catalytic mechanism of
both phosphorylation and
dephosphorylation.
REGION 264 269 Important for the catalytic mechanism of
dephosphorylation. {ECO:0000250}.
ACT_SITE 159 159 {ECO:0000250}.
ACT_SITE 177 177 Proton acceptor; for phosphorylation
activity. Proton donor; for
dephosphorylation activity.
{ECO:0000250}.
ACT_SITE 243 243 {ECO:0000250}.
METAL 138 138 Magnesium. {ECO:0000255}.
METAL 160 160 Magnesium. {ECO:0000305}.
METAL 202 202 Magnesium. {ECO:0000305}.
MUTAGEN 138 138 H->A: No effect on both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:12779331}.
MUTAGEN 148 148 G->A: Loss of both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:12055300}.
MUTAGEN 153 153 G->A: Loss of both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:12779331}.
MUTAGEN 155 155 S->A,T: Nearly no effect on both kinase
and phosphorylase activities.
{ECO:0000269|PubMed:12779331}.
MUTAGEN 155 155 S->C: Loss of both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:12779331}.
MUTAGEN 156 156 G->A: Loss of both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:12779331}.
MUTAGEN 158 158 G->A: Loss of both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:12779331}.
MUTAGEN 159 159 K->R: Slight reduction in both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:12779331}.
MUTAGEN 160 160 S->A: Loss of both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:12779331}.
MUTAGEN 160 160 S->T: Nearly no effect on both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:12779331}.
MUTAGEN 171 171 H->R: Loss of both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:12779331}.
MUTAGEN 202 202 E->A: No effect on ATP-dependent kinase
activity, but loss of both PPi-kinase and
phosphorylase activities.
MUTAGEN 204 204 R->A: Reduced kinase activity and loss of
phosphorylase activity.
MUTAGEN 205 205 G->A: No effect on ATP-dependent kinase
activity, but loss of both PPi-kinase and
phosphorylase activities.
MUTAGEN 207 207 G->A: Reduced kinase activity and loss of
phosphorylase activity. No effect on FBP
binding.
SEQUENCE 310 AA; 34702 MW; C44ABD220881EC31 CRC64;
MAKVRTKDVM EQFNLELISG EEGINRPITM SDLSRPGIEI AGYFTYYPRE RVQLLGKTEL
SFFEQLPEEE KKQRMDSLCT DVTPAIILSR DMPIPQELID ASEKNGVPVL RSPLKTTRLS
SRLTNFLESR LAPTTAIHGV LVDIYGVGVL ITGKSGVGKS ETALELVKRG HRLVADDCVE
IRQEDQDTLV GNAPELIEHL LEIRGLGIIN VMTLFGAGAV RSNKRITIVM NLELWEQGKQ
YDRLGLEEET MKIIDTEITK LTIPVRPGRN LAVIIEVAAM NFRLKRMGLN AAEQFTNKLA
DVIEDGEQEE


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