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Database: UniProt
Entry: A0A411HGN2_9GAMM
LinkDB: A0A411HGN2_9GAMM
Original site: A0A411HGN2_9GAMM 
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}.
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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
//
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