PPK11_CHLTE
ID PPK11_CHLTE Reviewed; 698 AA.
AC P58991;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Polyphosphate kinase 1 {ECO:0000255|HAMAP-Rule:MF_00347};
DE EC=2.7.4.1 {ECO:0000255|HAMAP-Rule:MF_00347};
DE AltName: Full=ATP-polyphosphate phosphotransferase 1 {ECO:0000255|HAMAP-Rule:MF_00347};
DE AltName: Full=Polyphosphoric acid kinase 1 {ECO:0000255|HAMAP-Rule:MF_00347};
GN Name=ppk1 {ECO:0000255|HAMAP-Rule:MF_00347}; Synonyms=ppk-1;
GN OrderedLocusNames=CT0887;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC of ATP to form a long-chain polyphosphate (polyP). {ECO:0000255|HAMAP-
CC Rule:MF_00347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP;
CC Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.4.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00347};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00347};
CC -!- PTM: An intermediate of this reaction is the autophosphorylated ppk in
CC which a phosphate is covalently linked to a histidine residue through a
CC N-P bond. {ECO:0000255|HAMAP-Rule:MF_00347}.
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 1 (PPK1) family.
CC {ECO:0000255|HAMAP-Rule:MF_00347}.
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DR EMBL; AE006470; AAM72122.1; -; Genomic_DNA.
DR RefSeq; NP_661780.1; NC_002932.3.
DR RefSeq; WP_010932567.1; NC_002932.3.
DR AlphaFoldDB; P58991; -.
DR SMR; P58991; -.
DR STRING; 194439.CT0887; -.
DR PRIDE; P58991; -.
DR EnsemblBacteria; AAM72122; AAM72122; CT0887.
DR KEGG; cte:CT0887; -.
DR PATRIC; fig|194439.7.peg.804; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_5_0_10; -.
DR OMA; NIKWARK; -.
DR OrthoDB; 76567at2; -.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0009358; C:polyphosphate kinase complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1840.10; -; 1.
DR HAMAP; MF_00347; Polyphosphate_kinase; 1.
DR InterPro; IPR003414; PP_kinase.
DR InterPro; IPR041108; PP_kinase_C_1.
DR InterPro; IPR024953; PP_kinase_middle.
DR InterPro; IPR036830; PP_kinase_middle_dom_sf.
DR InterPro; IPR025200; PPK_C_dom2.
DR InterPro; IPR025198; PPK_N_dom.
DR InterPro; IPR036832; PPK_N_dom_sf.
DR PANTHER; PTHR30218; PTHR30218; 1.
DR Pfam; PF02503; PP_kinase; 1.
DR Pfam; PF13090; PP_kinase_C; 1.
DR Pfam; PF17941; PP_kinase_C_1; 1.
DR Pfam; PF13089; PP_kinase_N; 1.
DR PIRSF; PIRSF015589; PP_kinase; 1.
DR SUPFAM; SSF140356; SSF140356; 1.
DR TIGRFAMs; TIGR03705; poly_P_kin; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..698
FT /note="Polyphosphate kinase 1"
FT /id="PRO_0000128638"
FT ACT_SITE 437
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 407
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 698 AA; 79347 MW; 3BA95EB9FBD1D165 CRC64;
MSDPSLYINR ELSWLHFNRR VLDEAIRQDQ HPLIERVKFI AIFSSNLDEF FMIRVAGIEK
QVEAGIRKKT IDGLTPSEQL ERIRAEVIEQ LKLRNTCLYG DILPALAAEG ITFVHFADLP
EKEQAVLNAW FRKEIYPVLT PLAFDTGHPF PFMSNLSLNL AIELDEVEHG NLKFARVKVP
SVLPRLLKLN DIEGLGNDPS CMRFLWIEEL IQQNLGLLFP TMKIVQSHQF RIIRNADIEI
EEDEAGDLLQ TIEKGVRSRR YGNVVRLDIS PEMPDFVRQL LINNLEIEEK NVYEIDGALG
MSCLMELLDI DRPSLKDEPF IPFNMFEEQR NGDIFSAISS GDLLFYHPYD SFKPVVDFID
RAASDPDVLS IKQTLYRVGS NSPIVKALMK AAESGKQVAV LVELKARFDE ENNIGWARAL
EDVGAHVIYG LPGLKTHAKL TLVVRREPQG LKRYLHLGTG NYNPSTGKLY TDYSFFTDDE
LLAGEVSELF NALTGYFRYT GYRFLLVSPI NTRKRIIEMI EREIALARKS SGGRIIMKMN
SLVDPATIQA LYRASRAGVQ IDLVVRGICC LKPGIPGVSE NIRVISIIGR YLEHSRAYYF
ANGGSPELYL GSADIMPRNL DDRVETLFPV FDPSLVERVR NDLELQLSDN LKAWKIGPDG
NWTLVRNDAP KVNSQERFMK RRTQKKKTTG IKGRLGLN
