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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_MYCPN              Reviewed;         312 AA.
P75548;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
07-JUN-2017, entry version 118.
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; OrderedLocusNames=MPN_223; ORFNames=MP608;
Mycoplasma pneumoniae (strain ATCC 29342 / M129).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=272634;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29342 / M129;
PubMed=8948633; DOI=10.1093/nar/24.22.4420;
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C.,
Herrmann R.;
"Complete sequence analysis of the genome of the bacterium Mycoplasma
pneumoniae.";
Nucleic Acids Res. 24:4420-4449(1996).
[2]
CHARACTERIZATION, AND MUTAGENESIS OF RESIDUES IN THE WALKER MOTIF A
AND IN THE HPRK/P SIGNATURE SEQUENCE.
PubMed=12368461;
Steinhauer K., Jepp T., Hillen W., Stuelke J.;
"A novel mode of control of Mycoplasma pneumoniae HPr
kinase/phosphatase activity reflects its parasitic lifestyle.";
Microbiology 148:3277-3284(2002).
[3]
CHARACTERIZATION, AND MUTAGENESIS OF GLY-154; GLY-159; LYS-160;
SER-161; ARG-204 AND GLY-207.
PubMed=14717704; DOI=10.1046/j.1432-1033.2003.03935.x;
Merzbacher M., Detsch C., Hillen W., Stuelke J.;
"Mycoplasma pneumoniae HPr kinase/phosphorylase.";
Eur. J. Biochem. 271:367-374(2004).
[4]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=12589763; DOI=10.1016/S0022-2836(02)01378-5;
Allen G.S., Steinhauer K., Hillen W., Stuelke J., Brennan R.G.;
"Crystal structure of HPr kinase/phosphatase from Mycoplasma
pneumoniae.";
J. Mol. Biol. 326:1203-1217(2003).
-!- FUNCTION: Is a metabolite-sensitive enzyme that catalyzes the ATP-
as well as probably the pyrophosphate-dependent phosphorylation of
Ser-47 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 regulatory role of
HPrK/P in the physiology of M.pneumoniae is not known yet.
-!- 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:0000250};
-!- ENZYME REGULATION: Contrary to HPrK/P of B.subtilis and other
bacteria, that of M.pneumoniae is active as a kinase at very low
ATP concentrations in the absence of fructose 1,6-bisphosphate
(FBP). Kinase activity is slightly activated by FBP, and inhibited
by inorganic phosphate (Pi), but FBP prevents kinase inhibition by
Pi. Dephosphorylation of P-Ser-HPr by M.pneumoniae HPrK/P is
strictly dependent on the presence of Pi, and is inhibited by FBP.
This unique mode of control of HPrK/P activity is proposed to
reflect the parasitic lifestyle of M.pneumoniae, that is strictly
adapted to its ecological niche on nutrient-rich human mucous
membranes.
-!- SUBUNIT: Homohexamer, arranged as bilayered trimers.
-!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
-!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried
out by the same active site and suggest a common mechanism for
both reactions.
-!- MISCELLANEOUS: Contrary to HPrK/P of other bacteria, that of
M.pneumoniae has a very high affinity for ATP (Kd=5.3 microM),
explaining kinase activity even at low ATP concentrations.
-!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000305}.
-!- CAUTION: Was originally (PubMed:12368461 and PubMed:12589763)
called HPr kinase/phosphatase, but P-Ser-HPr dephosphorylation was
shown in several bacteria to follow a quite unique mechanism, 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}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U00089; AAB96256.1; -; Genomic_DNA.
PIR; S73934; S73934.
RefSeq; NP_109911.1; NC_000912.1.
RefSeq; WP_010874580.1; NC_000912.1.
PDB; 1KNX; X-ray; 2.50 A; A/B/C/D/E/F=1-312.
PDBsum; 1KNX; -.
ProteinModelPortal; P75548; -.
SMR; P75548; -.
IntAct; P75548; 4.
EnsemblBacteria; AAB96256; AAB96256; MPN_223.
GeneID; 877117; -.
KEGG; mpn:MPN223; -.
PATRIC; fig|272634.6.peg.242; -.
KO; K06023; -.
OMA; IQKPGLA; -.
EvolutionaryTrace; P75548; -.
Proteomes; UP000000808; Chromosome.
GO; GO:0005622; C:intracellular; IEA:GOC.
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;
3D-structure; ATP-binding; Carbohydrate metabolism; Complete proteome;
Kinase; Magnesium; Metal-binding; Multifunctional enzyme;
Nucleotide-binding; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 312 HPr kinase/phosphorylase.
/FTId=PRO_0000058973.
NP_BIND 154 161 ATP. {ECO:0000305}.
REGION 201 210 Important for the catalytic mechanism of
both phosphorylation and
dephosphorylation.
REGION 266 271 Important for the catalytic mechanism of
dephosphorylation. {ECO:0000250}.
ACT_SITE 139 139 {ECO:0000250}.
ACT_SITE 160 160 {ECO:0000250}.
ACT_SITE 178 178 Proton acceptor; for phosphorylation
activity. Proton donor; for
dephosphorylation activity.
{ECO:0000250}.
ACT_SITE 245 245 {ECO:0000250}.
METAL 161 161 Magnesium. {ECO:0000305}.
METAL 202 202 Magnesium. {ECO:0000255}.
MUTAGEN 140 140 G->A: Kinase activity not affected and 6-
fold increase in phosphorylase activity.
{ECO:0000269|PubMed:12368461}.
MUTAGEN 154 154 G->A: 4-fold reduction in kinase activity
and loss of phosphorylase activity; 8-
fold reduction in ATP affinity.
{ECO:0000269|PubMed:14717704}.
MUTAGEN 156 156 S->A: Kinase activity not affected and 4-
fold increase in phosphorylase activity.
{ECO:0000269|PubMed:12368461}.
MUTAGEN 156 156 S->T: 4-fold reduction in kinase activity
and loss of phosphorylase activity.
{ECO:0000269|PubMed:12368461}.
MUTAGEN 157 157 G->A: 4-fold reduction in kinase activity
and strongly reduced phosphorylase
activity. {ECO:0000269|PubMed:12368461}.
MUTAGEN 159 159 G->A: Loss of both kinase and
phosphorylase activities; no ATP binding.
{ECO:0000269|PubMed:14717704}.
MUTAGEN 160 160 K->A: Loss of both kinase and
phosphorylase activities; no ATP binding.
{ECO:0000269|PubMed:14717704}.
MUTAGEN 160 160 K->R: Loss of both kinase and
phosphorylase activities.
{ECO:0000269|PubMed:14717704}.
MUTAGEN 161 161 S->A: 10-fold reduction in kinase
activity and loss of phosphorylase
activity; affinity for ATP is only
slightly affected.
{ECO:0000269|PubMed:14717704}.
MUTAGEN 161 161 S->T: 2-fold reduction in kinase activity
and strongly reduced phosphorylase
activity; binds ATP with high affinity.
{ECO:0000269|PubMed:14717704}.
MUTAGEN 162 162 E->D: Kinase activity not affected and
loss of phosphorylase activity.
{ECO:0000269|PubMed:12368461}.
MUTAGEN 204 204 R->K: Kinase activity not affected and
strongly reduced phosphorylase activity;
ATP binding not affected.
{ECO:0000269|PubMed:14717704}.
MUTAGEN 207 207 G->A: Loss of both kinase and
phosphorylase activities; ATP binding not
affected. {ECO:0000269|PubMed:14717704}.
HELIX 6 10 {ECO:0000244|PDB:1KNX}.
TURN 14 16 {ECO:0000244|PDB:1KNX}.
HELIX 39 42 {ECO:0000244|PDB:1KNX}.
STRAND 54 56 {ECO:0000244|PDB:1KNX}.
HELIX 58 64 {ECO:0000244|PDB:1KNX}.
HELIX 69 72 {ECO:0000244|PDB:1KNX}.
TURN 73 75 {ECO:0000244|PDB:1KNX}.
HELIX 76 80 {ECO:0000244|PDB:1KNX}.
STRAND 87 90 {ECO:0000244|PDB:1KNX}.
TURN 91 93 {ECO:0000244|PDB:1KNX}.
HELIX 97 102 {ECO:0000244|PDB:1KNX}.
HELIX 103 105 {ECO:0000244|PDB:1KNX}.
STRAND 110 115 {ECO:0000244|PDB:1KNX}.
HELIX 117 120 {ECO:0000244|PDB:1KNX}.
TURN 121 123 {ECO:0000244|PDB:1KNX}.
HELIX 124 131 {ECO:0000244|PDB:1KNX}.
STRAND 136 145 {ECO:0000244|PDB:1KNX}.
STRAND 148 159 {ECO:0000244|PDB:1KNX}.
HELIX 160 168 {ECO:0000244|PDB:1KNX}.
TURN 169 171 {ECO:0000244|PDB:1KNX}.
STRAND 173 185 {ECO:0000244|PDB:1KNX}.
STRAND 188 193 {ECO:0000244|PDB:1KNX}.
TURN 195 199 {ECO:0000244|PDB:1KNX}.
STRAND 200 203 {ECO:0000244|PDB:1KNX}.
TURN 204 206 {ECO:0000244|PDB:1KNX}.
STRAND 207 210 {ECO:0000244|PDB:1KNX}.
HELIX 211 215 {ECO:0000244|PDB:1KNX}.
HELIX 217 219 {ECO:0000244|PDB:1KNX}.
STRAND 224 233 {ECO:0000244|PDB:1KNX}.
STRAND 252 255 {ECO:0000244|PDB:1KNX}.
STRAND 258 266 {ECO:0000244|PDB:1KNX}.
HELIX 273 288 {ECO:0000244|PDB:1KNX}.
HELIX 293 304 {ECO:0000244|PDB:1KNX}.
HELIX 305 308 {ECO:0000244|PDB:1KNX}.
SEQUENCE 312 AA; 35234 MW; 475F6B73587517C1 CRC64;
MKKLLVKELI EQFQDCVNLI DGHTNTSNVI RVPGLKRVVF EMLGLFSSQI GSVAILGKRE
FGFLSQKTLV EQQQILHNLL KLNPPAIILT KSFTDPTVLL QVNQTYQVPI LKTDFFSTEL
SFTVETYINE QFATVAQIHG VLLEVFGVGV LLTGRSGIGK SECALDLINK NHLFVGDDAI
EIYRLGNRLF GRAQEVAKKF MEIRGLGIIN VERFYGLQIT KQRTEIQLMV NLLSLEKQTT
VTFERLGTEL KKQRLLGVDL SFYEIPISPG RKTSEIIESA VIDFKLKHSG YNSALDFIEN
QKAILKRKKD ES


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