ID   HPRK_FUSNN              Reviewed;         615 AA.
AC   Q8R5N8;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Putative HPr kinase/phosphorylase;
DE            Short=HPrK/P;
DE            EC=2.7.11.-;
DE            EC=2.7.4.-;
GN   Name=hprK; OrderedLocusNames=FN1012;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
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) (By similarity). {ECO:0000250}.
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   -!- 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;
CC   -!- MISCELLANEOUS: This protein is composed of two complete HPrK/P domains
CC       fused in tandem. This unusual organization may lead to a separation of
CC       the two antagonistic activities in F.nucleatum, with the C-terminal
CC       copy carrying the kinase and the N-terminal copy carrying the
CC       phosphorylase.
CC   -!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000305}.
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DR   EMBL; AE009951; AAL95208.1; -; Genomic_DNA.
DR   RefSeq; NP_603909.3; NC_003454.1.
DR   AlphaFoldDB; Q8R5N8; -.
DR   SMR; Q8R5N8; -.
DR   STRING; 190304.FN1012; -.
DR   PRIDE; Q8R5N8; -.
DR   EnsemblBacteria; AAL95208; AAL95208; FN1012.
DR   KEGG; fnu:FN1012; -.
DR   PATRIC; fig|190304.8.peg.1577; -.
DR   eggNOG; COG1493; Bacteria.
DR   HOGENOM; CLU_031537_0_0_0; -.
DR   InParanoid; Q8R5N8; -.
DR   OMA; LIHRGHR; -.
DR   BioCyc; FNUC190304:G1FZS-1594-MON; -.
DR   Proteomes; UP000002521; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006109; P:regulation of carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd01918; HprK_C; 2.
DR   Gene3D; 3.40.1390.20; -; 2.
DR   Gene3D; 3.40.50.300; -; 2.
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   PANTHER; PTHR30305:SF1; PTHR30305:SF1; 2.
DR   Pfam; PF07475; Hpr_kinase_C; 2.
DR   Pfam; PF02603; Hpr_kinase_N; 2.
DR   SUPFAM; SSF75138; SSF75138; 2.
DR   TIGRFAMs; TIGR00679; hpr-ser; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Multifunctional enzyme; Nucleotide-binding;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..615
FT                   /note="Putative HPr kinase/phosphorylase"
FT                   /id="PRO_0000059010"
FT   BINDING         480..487
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   615 AA;  70671 MW;  F7124DE79F9A15BD CRC64;
     MYTYTTIREI VDKLNLEILN EGNLDLKIDI PNIYQIGYEL VGFLDKESDE LNKYINICSL
     KESRFIATFS KERKEKVISE YMSLDFPALI FTKDAIITEE FYYYAKRYNK NILLSNEKAS
     VTVRKIKFFL SKALSIEEEY ENYSLMEIHG VGVLMSGYSN ARKGVMIELI ERGHRMVTDK
     NLIIRRVGEN DLVGYNAKKR EKLGHFYLED IKGGYVDVTD HFGVKSTRIE KKINILIVLE
     EWNEKEFYDR LGLDVQYEDF VGEKIQKYII PVRKGRNLAV IIETAALTFR LRRMGHNTPL
     EFLTKSQEII ERKKKEREEY MNTNRLPVTK LINEFDLEIK YGEDKVSSTY INSSNVYRPS
     LSLIGFFDLI EEVKNIGIQI FSKIEFKFLE NLPPIERVNN LKKFLTYDIP MIVLTVDANP
     PDYFFDLVSK SGHILAIAPY KKASQIVANF NNYLDSFFSE TTSVHGVLVE LFGFGVLLTG
     KSGIGKSETA LELIHRGHRL IADDMVKFYR NTQGDVVGKS AELPFFMEIR GLGIIDIKTL
     YGLSAVRLSK TLDMIIELQA VDNSDYMSAP SAHLYEDVLG KPIKKRILEI SSGRNAAAMV
     EVMVMDHMSG LLGEK