ID A0A411HGN2_9GAMM Unreviewed; 319 AA.
AC A0A411HGN2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=HPr kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249};
DE Short=HPrK/P {ECO:0000256|HAMAP-Rule:MF_01249};
DE EC=2.7.11.- {ECO:0000256|HAMAP-Rule:MF_01249};
DE EC=2.7.4.- {ECO:0000256|HAMAP-Rule:MF_01249};
DE AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249};
GN Name=hprK {ECO:0000256|HAMAP-Rule:MF_01249,
GN ECO:0000313|EMBL:QBB69643.1};
GN ORFNames=ELE36_04210 {ECO:0000313|EMBL:QBB69643.1};
OS Pseudolysobacter antarcticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudolysobacter.
OX NCBI_TaxID=2511995 {ECO:0000313|EMBL:QBB69643.1, ECO:0000313|Proteomes:UP000291562};
RN [1] {ECO:0000313|EMBL:QBB69643.1, ECO:0000313|Proteomes:UP000291562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AQ6-296 {ECO:0000313|EMBL:QBB69643.1,
RC ECO:0000313|Proteomes:UP000291562};
RA Wei Z., Peng F.;
RT "Pseudolysobacter antarctica gen. nov., sp. nov., isolated from Fildes
RT Peninsula, Antarctica.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent
CC phosphorylation of a specific serine residue in HPr, a phosphocarrier
CC protein of the phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (PTS). HprK/P also catalyzes the pyrophosphate-producing,
CC inorganic phosphate-dependent dephosphorylation (phosphorolysis) of
CC seryl-phosphorylated HPr (P-Ser-HPr). {ECO:0000256|HAMAP-
CC Rule:MF_01249}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-
CC serine + ADP + H(+); Xref=Rhea:RHEA:46600, Rhea:RHEA-COMP:11602,
CC Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001120, ECO:0000256|HAMAP-
CC Rule:MF_01249};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[HPr protein]-O-phospho-L-serine + H(+) + phosphate = [HPr
CC protein]-L-serine + diphosphate; Xref=Rhea:RHEA:46604, Rhea:RHEA-
CC COMP:11602, Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; Evidence={ECO:0000256|ARBA:ARBA00001319,
CC ECO:0000256|HAMAP-Rule:MF_01249};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01249};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01249}.
CC -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
CC {ECO:0000256|HAMAP-Rule:MF_01249}.
CC -!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried out
CC by the same active site and suggest a common mechanism for both
CC reactions. {ECO:0000256|HAMAP-Rule:MF_01249}.
CC -!- SIMILARITY: Belongs to the HPrK/P family.
CC {ECO:0000256|ARBA:ARBA00006883, ECO:0000256|HAMAP-Rule:MF_01249}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP035704; QBB69643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411HGN2; -.
DR KEGG; xbc:ELE36_04210; -.
DR OrthoDB; 9778803at2; -.
DR Proteomes; UP000291562; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01918; HprK_C; 1.
DR Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01249; HPr_kinase; 1.
DR InterPro; IPR003755; HPr(Ser)_kin/Pase.
DR InterPro; IPR011104; Hpr_kin/Pase_C.
DR InterPro; IPR011126; Hpr_kin/Pase_Hpr_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR NCBIfam; TIGR00679; hpr-ser; 1.
DR PANTHER; PTHR30305:SF1; HPR KINASE/PHOSPHORYLASE; 1.
DR PANTHER; PTHR30305; UNCHARACTERIZED; 1.
DR Pfam; PF07475; Hpr_kinase_C; 1.
DR Pfam; PF02603; Hpr_kinase_N; 1.
DR SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01249};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01249};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01249};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01249};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01249};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01249}; Reference proteome {ECO:0000313|Proteomes:UP000291562};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|HAMAP-Rule:MF_01249};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01249}.
FT DOMAIN 7..131
FT /note="HPr(Ser) kinase/phosphorylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02603"
FT DOMAIN 135..308
FT /note="HPr kinase/phosphorylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07475"
FT REGION 205..214
FT /note="Important for the catalytic mechanism of both
FT phosphorylation and dephosphorylation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT REGION 274..279
FT /note="Important for the catalytic mechanism of
FT dephosphorylation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 142
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 163
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 181
FT /note="Proton acceptor; for phosphorylation activity.
FT Proton donor; for dephosphorylation activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT ACT_SITE 253
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
SQ SEQUENCE 319 AA; 35909 MW; C4EC36F3E69F6D84 CRC64;
MDRLTARELF DSVAERLGLR WIAGLNGGSR AIEPAEKQSR RPSLVGYLNV IYPNKLQIIG
TEELNFLDSL DSRQRWDVIQ KIMAYKPTAL VVTKDQKIPS DMREAADETA TPLWSSPNRG
HELYTYLHYH LARLLANKVT LHGVLMEVYS IGVLITGESG SGKSELALEL LTRGHRLVAD
DAPEFTQIAP DVVDGNCPEM LQDFLEVRGL GILNIREMFG HTAVKQSKYL RLIVHLTPLL
LDDANRDRDG LKRLYGDVSY REVLGVQIPQ MMIPVAPGRN LAVLVEAAVR SHMLRTKGID
PAQTFIDRQA HQMKRQAPW
//