PPK1_NEIMB
ID PPK1_NEIMB Reviewed; 685 AA.
AC Q9JXS9; Q59616;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Polyphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00347};
DE EC=2.7.4.1 {ECO:0000255|HAMAP-Rule:MF_00347};
DE AltName: Full=ATP-polyphosphate phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00347};
DE AltName: Full=Polyphosphoric acid kinase {ECO:0000255|HAMAP-Rule:MF_00347};
GN Name=ppk {ECO:0000255|HAMAP-Rule:MF_00347}; OrderedLocusNames=NMB1900;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BNCV / Serogroup B;
RX PubMed=7729865; DOI=10.1128/iai.63.5.1624-1630.1995;
RA Tinsley C.R., Gotschlich E.C.;
RT "Cloning and characterization of the meningococcal polyphosphate kinase
RT gene: production of polyphosphate synthesis mutants.";
RL Infect. Immun. 63:1624-1630(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-208.
RX PubMed=9501229; DOI=10.1073/pnas.95.6.3140;
RA Maiden M.C.J., Bygraves J.A., Feil E., Morelli G., Russell J.E., Urwin R.,
RA Zhang Q., Zhou J., Zurth K., Caugant D.A., Feavers I.M., Achtman M.,
RA Spratt B.G.;
RT "Multilocus sequence typing: a portable approach to the identification of
RT clones within populations of pathogenic microorganisms.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3140-3145(1998).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF42231.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE002098; AAF42231.1; ALT_INIT; Genomic_DNA.
DR EMBL; U16262; AAA85674.1; -; Genomic_DNA.
DR EMBL; AF037931; AAC08915.1; -; Genomic_DNA.
DR PIR; B81030; B81030.
DR RefSeq; NP_274895.1; NC_003112.2.
DR RefSeq; WP_002225804.1; NC_003112.2.
DR AlphaFoldDB; Q9JXS9; -.
DR SMR; Q9JXS9; -.
DR STRING; 122586.NMB1900; -.
DR PaxDb; Q9JXS9; -.
DR EnsemblBacteria; AAF42231; AAF42231; NMB1900.
DR KEGG; nme:NMB1900; -.
DR PATRIC; fig|122586.8.peg.2425; -.
DR HOGENOM; CLU_009678_5_0_4; -.
DR OMA; AHPFPQV; -.
DR Proteomes; UP000000425; 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..685
FT /note="Polyphosphate kinase"
FT /id="PRO_0000128651"
FT ACT_SITE 435
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 375
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 405
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT CONFLICT 28
FT /note="Q -> K (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..66
FT /note="HKRCPQ -> NKLHPR (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..109
FT /note="QEG -> RES (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="D -> G (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="A -> R (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="A -> D (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="L -> I (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="I -> T (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="V -> I (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="Y -> C (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="T -> A (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="T -> A (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="T -> A (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="H -> R (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="T -> E (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="D -> A (in Ref. 2; AAA85674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 685 AA; 77258 MW; 192D5B8F5B6370D6 CRC64;
MPEQNRILCR ELSLLAFNRR VLAQAEDQNV PLLERLRFLC IVSSNLDEFF EVRMAWLKRE
HKRCPQRRLD NGKMPSETIA DVTEAARSLI RHQYDLFNNV LQPELAQEGI HFYRRRNWTD
TQKKWIEDYF DRELLPILTP IGLDPSHPFP RPLNKSLNFA VELDGTDAFG RPSGMAIVQA
PRILPRVVPL PSELCGGGHG FVFLSSILHA HVGKLFPGMN VKGCHQFRLT RDSDLTVDEE
DLQNLRAAIQ NELHDREYGD GVRLEVADTC PAYIRDFLLA QFKLTAAELY QVKGPVNLVR
LNAVPDLVNR PDLKFPTHTP GRLKALGKTA SIFDLVRQSP ILLHHPYQSF DPVVEMMREA
AADPAVLAVK MTIYRTGTRS ELVRALMKAA LAGKQVTVVV ELMARFDEAN NVNWAKQLEE
AGAHVVYGVF GYKVHAKMAL VIRREDGVLK RYAHLGTGNY HQGTSRIYTD FGLITADEQI
TADVNILFME ITGLGKPGRL NKLYQSPFTL HKMVIDRIAR ETEHAKAGKP ARITAKMNSL
IEPTVIEALY RASAAGVQID LIVRGMCTLR PGVKGLSENI RVRSIVGRQL EHARVYYFHN
NGTDDTFISS ADWMGRNFFR RIETATPITA PELKKRVIHE GLTMALDDNT HAWLMQPDGG
YIRAAPAEGE SEADLQNDLW TLLGG
