PPK12_CHLTE
ID PPK12_CHLTE Reviewed; 714 AA.
AC O68984;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Polyphosphate kinase 2 {ECO:0000255|HAMAP-Rule:MF_00347};
DE EC=2.7.4.1 {ECO:0000255|HAMAP-Rule:MF_00347};
DE AltName: Full=ATP-polyphosphate phosphotransferase 2 {ECO:0000255|HAMAP-Rule:MF_00347};
DE AltName: Full=Polyphosphoric acid kinase 2 {ECO:0000255|HAMAP-Rule:MF_00347};
GN Name=ppk2 {ECO:0000255|HAMAP-Rule:MF_00347}; Synonyms=ppk, ppk-2;
GN OrderedLocusNames=CT1049;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131.
RA Bryant D.A., Jakobs C., Stirewalt V.L.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
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; AAM72282.1; -; Genomic_DNA.
DR EMBL; AF060078; AAC14871.1; -; Genomic_DNA.
DR RefSeq; NP_661940.1; NC_002932.3.
DR RefSeq; WP_010932727.1; NC_002932.3.
DR AlphaFoldDB; O68984; -.
DR SMR; O68984; -.
DR STRING; 194439.CT1049; -.
DR EnsemblBacteria; AAM72282; AAM72282; CT1049.
DR KEGG; cte:CT1049; -.
DR PATRIC; fig|194439.7.peg.955; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_5_0_10; -.
DR OMA; AHPFPQV; -.
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..714
FT /note="Polyphosphate kinase 2"
FT /id="PRO_0000128639"
FT ACT_SITE 455
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 395
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 425
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 714 AA; 81891 MW; CCF402FB4D2CB98A CRC64;
MTDSENGTLV PAAIAEPDLR DPLLYVNREL SWIDFNQRVL EEALDSAAHP LLERVKFLSI
FSSNLDEFFM IRVAGLDDQC AAGINERSVD GLTPIEMLER IRERVIGQLR QRNACFFDDI
LPALKRKGIE FVSVSSLSVE QQQLLQHYFR KEVFPVLTPL AFDTGHPFPF MSNLSLNLAI
ELEDEESGAI KFARVKVPGI LSRIIRLDQI EGLGFDDGRI RLLWLEDLVE HNLDQLFPKM
RILQCHPFRI IRDADIEIEE DEAGDLLESI EQGVRSRRYG KVVRLDINPD MPHSIRSLLV
KNLETYERNV YEIGGVLGMS ALMELLKIDR PDLKDELFVP NNPLDDKRTA DIFAEMRSGD
MLLHHPYDSF KPVVDLIWQA ARDPDVLSIK QTLYRVGSNS PVVKALMFAA EQRKQVAVLV
ELKARFDEEN NILWARSLED AGAHVVYGLP GLKTHAKLTM IVRREQEGLR HYLHLGTGNY
NTVTARIYTD YSYLTTDPVL ADDVTELFNS LTGYSKHREY RSLIVSPLNM RRWIMEMIRH
EVDHQKHTGN GRIVMKMNAL VDEEIIRALY RASMAGVKID LAIRGICCLK PGIPGISENI
RVVSVIGRFL EHSRVYYFNN GDHARIFLGS ADIMPRNLDK RVETLFPVIE PRLVESIKSD
LELTLSDNRK SWEMQPDGTY IRKRGGRPAV DSQRLFMRRS LRRKKNIKKK VKGL
