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Database: UniProt
Entry: A0A0R2A7M7_9LACO
LinkDB: A0A0R2A7M7_9LACO
Original site: A0A0R2A7M7_9LACO 
ID   A0A0R2A7M7_9LACO        Unreviewed;       310 AA.
AC   A0A0R2A7M7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=HPr kinase/phosphorylase {ECO:0000256|ARBA:ARBA00018922, 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|ARBA:ARBA00033012, ECO:0000256|HAMAP-Rule:MF_01249};
GN   Name=hprK {ECO:0000256|HAMAP-Rule:MF_01249};
GN   ORFNames=FC14_GL000492 {ECO:0000313|EMBL:KRM63457.1};
OS   Ligilactobacillus agilis DSM 20509.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1423718 {ECO:0000313|EMBL:KRM63457.1, ECO:0000313|Proteomes:UP000051008};
RN   [1] {ECO:0000313|EMBL:KRM63457.1, ECO:0000313|Proteomes:UP000051008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20509 {ECO:0000313|EMBL:KRM63457.1,
RC   ECO:0000313|Proteomes:UP000051008};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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). The two antagonistic activities
CC       of HprK/P are regulated by several intracellular metabolites, which
CC       change their concentration in response to the absence or presence of
CC       rapidly metabolisable carbon sources (glucose, fructose, etc.) in the
CC       growth medium. Therefore, by controlling the phosphorylation state of
CC       HPr, HPrK/P is a sensor enzyme that plays a major role in the
CC       regulation of carbon metabolism and sugar transport: it mediates carbon
CC       catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate
CC       uptake and inducer exclusion. {ECO:0000256|HAMAP-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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRM63457.1}.
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DR   EMBL; AYYP01000061; KRM63457.1; -; Genomic_DNA.
DR   RefSeq; WP_056977145.1; NZ_AYYP01000061.1.
DR   AlphaFoldDB; A0A0R2A7M7; -.
DR   PATRIC; fig|1423718.3.peg.511; -.
DR   OrthoDB; 9778803at2; -.
DR   Proteomes; UP000051008; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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   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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01249};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, 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:UP000051008};
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          4..128
FT                   /note="HPr(Ser) kinase/phosphorylase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02603"
FT   DOMAIN          131..299
FT                   /note="HPr kinase/phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07475"
FT   REGION          202..211
FT                   /note="Important for the catalytic mechanism of both
FT                   phosphorylation and dephosphorylation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT   REGION          265..270
FT                   /note="Important for the catalytic mechanism of
FT                   dephosphorylation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT   ACT_SITE        160
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT   ACT_SITE        178
FT                   /note="Proton acceptor; for phosphorylation activity.
FT                   Proton donor; for dephosphorylation activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT   BINDING         154..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01249"
SQ   SEQUENCE   310 AA;  34661 MW;  BB36ECB9C4DD5D69 CRC64;
     MNKVSVAELV DANGLIVYSG GMYLKERFIT TSDISRPGLE LTGYFDYYPE ERVQLMGMTE
     ISYAHKMEPA ARKEIMERMC GENTPCFVIS RYLSVPEEME QAAKEHQIPI LRSKLPTTRL
     SSKLTDYLES KLAERKSLHG VLVDIYGLGV LITGDSGVGK SETALDLIKR GHRLIADDRV
     EVYQQDEQTI IGEAPKILQH LLEIRGVGII DVMNLFGAGA VRTSTDISLI VHLENWSKDK
     QFDRLGSGEQ SVQIFDVAIP KITIPVKVGR NMAIIIEAAA MNYRAKTMGY DATKAFERNL
     NSLIQENSQD
//
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