GCW_04025







Uniprot: A0A0F6CLI9
Description: HPr kinase
EC number: 2.7.11.-; 2.7.4.-
Annotation score: 3 out of 5
Miscellaneous [CC]: 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}.
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: ATP + HPr = ADP + P-Ser-HPr. {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00281214}.; CATALYTIC ACTIVITY: P-Ser-HPr + phosphate = HPr + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00281211}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00281221};
Enzyme regulation: 
Function [CC]: 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). {ECO:0000256|HAMAP-Rule:MF_01249}.
Pathway: 
Active site: ACT_SITE 139 139 {ECO:0000256|HAMAP-Rule:MF_01249}.; ACT_SITE 160 160 {ECO:0000256|HAMAP-Rule:MF_01249}.; ACT_SITE 178 178 Proton acceptor; for phosphorylation activity. Proton donor; for dephosphorylation activity. {ECO:0000256|HAMAP-Rule:MF_01249}.; ACT_SITE 245 245 {ECO:0000256|HAMAP-Rule:MF_01249}.
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: METAL 161 161 Magnesium. {ECO:0000256|HAMAP-Rule:MF_01249}.; METAL 202 202 Magnesium. {ECO:0000256|HAMAP-Rule:MF_01249}.
Nucleotide binding: NP_BIND 154 161 ATP. {ECO:0000256|HAMAP-Rule:MF_01249}.
Site: 
Gene names (primary): hprK
Gene names (synonym): 
Mass: 35,603
Subunit structure [CC]: SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00281210}.
Gene ontology (GO): intracellular [GO:0005622]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phosphorelay sensor kinase activity [GO:0000155]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; regulation of carbohydrate metabolic process [GO:0006109]
Gene ontology IDs: GO:0000155; GO:0000287; GO:0004674; GO:0004712; GO:0005524; GO:0005622; GO:0006109
Chain: 
Signal peptide: 
Domain [CC]: DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi. {ECO:0000256|HAMAP-Rule:MF_01249}.
Sequence similarities: SIMILARITY: Belongs to the HPrK/P family. {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00535415}.
Protein families: HPrK/P family
Coiled coil: 
Domain [FT]: DOMAIN 4 125 Hpr_kinase_N. {ECO:0000259|Pfam:PF02603}.; DOMAIN 130 301 Hpr_kinase_C. {ECO:0000259|Pfam:PF07475}.
Motif: 
Region: REGION 201 210 Important for the catalytic mechanism of both phosphorylation and dephosphorylation. {ECO:0000256|HAMAP-Rule:MF_01249}.; REGION 266 271 Important for the catalytic mechanism of dephosphorylation. {ECO:0000256|HAMAP-Rule:MF_01249}.
EMBL: CP006916
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: AHB99961
UniPathway: K06023
CDD: 
Gene3D: 
HAMAP: 3.40.1390.20;3.40.50.300
InterPro: MF_01249
PANTHER: IPR003755;IPR011104;IPR011126;IPR027417;IPR028979
PIRSF: 
PRINTS: 
PROSITE: 
Pfam: 
ProDom: PF07475;PF02603
SMART: 
SUPFAM: 
TIGRFAMs: SSF75138
971503-972436(-)

>nucleotide sequence
TTATTCTTCCTTTGTCATGTATTTGTAATAACGTTCAACAAAATCATCCCCAGAGTTATA
TTGTCAATCACGTTTTAGTTTTAGATCAATAACTGCGCTTTCAATTAGTTCACTACTTCT
ACGACCTGAACTAATTGGTAAAACGTAATGAGGAACTTTAATATTTTCAATCACTTTATA
CCGTGTTTTTTGACCGGTTCGTTCGAAATTATAAGGTTGGTTATTTTGAATATTAATTAG
TTCAACAACTATTGAAATATGGGCTGATGATTTAATCTTTTCAATTCCATACATCTTAGT
AACATTTAAGATTCCAATCCCTCTAACTTCAATAAAGTGTTTGTTAATCTCGGTTGGTCG
TCCGATTAAACGGTCACCGATTCTGGCAATTGAAATTGCATCATCGGCGACAAATAAAAA
GTTTTTGCGAAGCATCTCCATCGCTACTTCGGATTTACCAATTCCAGATTCTCCTATAAT
TAGAACCCCTTCACCATATACTTCTATTAAGACACCATGGTGAATTGTGTATTTGGCAAG
TTGTTTAGAGATATAAAGACCAATCGAGATATTTAATTCGTTAGAATACATATCTGTACA
AAGAATTGGGACTTTATATTCTTTGTTACATTCTTTTAAGAAGACTGGATCTAGGAATGA
CTTGGTTAAGATTAAAACTGGTGGTTGTAATTCCAATAATCTTTTTGTTTTTTCTTTTCT
TTCTTCTGGAGATAAAGAAGTTAGATAAGAATATTCTCGGTTACCAAGAACAACGGCGCT
TTTAATTGGATCTGATTGAAACGAACCAAATAGTTCGAATGTGGGTCTTGATAGCCCTGG
CTTTTCAATTACCCGATCCATGTTTTCTTCACCATCTAGGATTACTAAGATGACTTCAAA
CTTATCGTATATATCTTTTACTGTAAAACTCAA


>protein sequence
LSFTVKDIYDKFEVILVILDGEENMDRVIEKPGLSRPTFELFGSFQSDPIKSAVVLGNRE
YSYLTSLSPEERKEKTKRLLELQPPVLILTKSFLDPVFLKECNKEYKVPILCTDMYSNEL
NISIGLYISKQLAKYTIHHGVLIEVYGEGVLIIGESGIGKSEVAMEMLRKNFLFVADDAI
SIARIGDRLIGRPTEINKHFIEVRGIGILNVTKMYGIEKIKSSAHISIVVELINIQNNQP
YNFERTGQKTRYKVIENIKVPHYVLPISSGRRSSELIESAVIDLKLKRDWQYNSGDDFVE
RYYKYMTKEE






















© Fisunov Lab of Proteomics, 2016.