UniProtKB - Q9S1H5 (HPRK_STAXY)
Protein
HPr kinase/phosphorylase
Gene
hprK
Organism
Staphylococcus xylosus
Status
Functioni
Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of 'Ser-46' 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. Therefore, by controlling the phosphorylation state of HPr, the 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.
Miscellaneous
Both phosphorylation and phosphorolysis are carried out by the same active site and suggest a common mechanism for both reactions.By similarity
Caution
Was originally (PubMed:10714994 and PubMed:11904409) called HPr kinase/phosphatase, but P-Ser-HPr dephosphorylation was shown (PubMed:12359880) to follow a quite unique mechanism, in which Pi instead of H2O is used for the nucleophilic attack on the phosphoryl group. P-Ser-HPr dephosphorylation is therefore not a phosphohydrolysis but a phospho-phosphorolysis reaction, and the bifunctional enzyme was dubbed HPr kinase/phosphorylase.1 Publication
Catalytic activityi
Cofactori
Mg2+By similarity
Activity regulationi
Kinase activity is activated by fructose 1,6-bisphosphate (FBP) only at low concentrations of enzyme or at high ATP concentrations.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 136 | By similarity | 1 | |
Active sitei | 157 | By similarity | 1 | |
Metal bindingi | 158 | MagnesiumSequence analysis | 1 | |
Active sitei | 175 | Proton acceptor; for phosphorylation activity. Proton donor; for dephosphorylation activityBy similarity | 1 | |
Metal bindingi | 200 | MagnesiumSequence analysis | 1 | |
Active sitei | 241 | By similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 151 – 158 | ATPCurated | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-UniRule
- magnesium ion binding Source: UniProtKB-UniRule
- phosphorelay sensor kinase activity Source: InterPro
- protein serine/threonine/tyrosine kinase activity Source: UniProtKB-UniRule
- protein serine/threonine kinase activity Source: UniProtKB-KW
GO - Biological processi
- carbohydrate metabolic process Source: UniProtKB-KW
- regulation of carbohydrate metabolic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Kinase, Multifunctional enzyme, Serine/threonine-protein kinase, Transferase |
Biological process | Carbohydrate metabolism |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:hprK |
Organismi | Staphylococcus xylosus |
Taxonomic identifieri | 1288 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000058991 | 1 – 314 | HPr kinase/phosphorylaseAdd BLAST | 314 |
Expressioni
Inductioni
Constitutively expressed, with or without glucose in the growth medium.
Interactioni
Subunit structurei
Homohexamer, arranged as bilayered trimers.
Protein-protein interaction databases
STRINGi | 1288.SXYLSMQ121_1936 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q9S1H5 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9S1H5 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 199 – 208 | Important for the catalytic mechanism of both phosphorylation and dephosphorylationBy similarity | 10 | |
Regioni | 262 – 267 | Important for the catalytic mechanism of dephosphorylationBy similarity | 6 |
Domaini
The Walker A ATP-binding motif also binds Pi and PPi.Curated
Sequence similaritiesi
Belongs to the HPrK/P family.Curated
Phylogenomic databases
eggNOGi | COG1493, Bacteria |
OrthoDBi | 391150at2 |
Family and domain databases
CDDi | cd01918, HprK_C, 1 hit |
Gene3Di | 3.40.1390.20, 1 hit |
HAMAPi | MF_01249, HPr_kinase, 1 hit |
InterProi | View protein in InterPro IPR003755, HPr(Ser)_kin/Pase IPR011104, Hpr_kin/Pase_C IPR011126, Hpr_kin/Pase_Hpr_N IPR028979, Ser_kin/Pase_Hpr-like_N_sf |
PANTHERi | PTHR30305:SF1, PTHR30305:SF1, 1 hit |
Pfami | View protein in Pfam PF07475, Hpr_kinase_C, 1 hit PF02603, Hpr_kinase_N, 1 hit |
SUPFAMi | SSF75138, SSF75138, 1 hit |
TIGRFAMsi | TIGR00679, hpr-ser, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9S1H5-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLTTKSLVER FELEMIAGEA GLNKQIKNTD ISRPGLEMAG YFSHYASDRI
60 70 80 90 100
QLLGTTELSF YNLLPDEERK GRMRKLCRPE TPAIIVTRDL EPPEELIEAA
110 120 130 140 150
KEHETPLITS KIATTQLMSR LTTFLEHELA RTTSLHGVLV DVYGVGVLIT
160 170 180 190 200
GDSGIGKSET ALELIKRGHR LVADDNVEIR EISKDELIGR APKLIEHLLE
210 220 230 240 250
IRGLGIINVM TLFGAGSILT EKRLRLNIHL ENWHKEKLYD RVGLNEETLR
260 270 280 290 300
ILDTEITKKT IPVRPGRNVA VIIEVAAMNY RLNIMGINTA EEFNDRLNAE
310
ILRNGNNGNN GEEK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ243915 Genomic DNA Translation: CAB51944.1 |
RefSeqi | WP_042363085.1, NZ_VBTJ01000001.1 |
Genome annotation databases
GeneIDi | 45497584 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ243915 Genomic DNA Translation: CAB51944.1 |
RefSeqi | WP_042363085.1, NZ_VBTJ01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1KO7 | X-ray | 1.95 | A/B | 1-314 | [»] | |
SMRi | Q9S1H5 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 1288.SXYLSMQ121_1936 |
Genome annotation databases
GeneIDi | 45497584 |
Phylogenomic databases
eggNOGi | COG1493, Bacteria |
OrthoDBi | 391150at2 |
Miscellaneous databases
EvolutionaryTracei | Q9S1H5 |
Family and domain databases
CDDi | cd01918, HprK_C, 1 hit |
Gene3Di | 3.40.1390.20, 1 hit |
HAMAPi | MF_01249, HPr_kinase, 1 hit |
InterProi | View protein in InterPro IPR003755, HPr(Ser)_kin/Pase IPR011104, Hpr_kin/Pase_C IPR011126, Hpr_kin/Pase_Hpr_N IPR028979, Ser_kin/Pase_Hpr-like_N_sf |
PANTHERi | PTHR30305:SF1, PTHR30305:SF1, 1 hit |
Pfami | View protein in Pfam PF07475, Hpr_kinase_C, 1 hit PF02603, Hpr_kinase_N, 1 hit |
SUPFAMi | SSF75138, SSF75138, 1 hit |
TIGRFAMsi | TIGR00679, hpr-ser, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HPRK_STAXY | |
Accessioni | Q9S1H5Primary (citable) accession number: Q9S1H5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 10, 2004 |
Last sequence update: | May 1, 2000 | |
Last modified: | August 12, 2020 | |
This is version 96 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families