ID   PK21_MYCS2              Reviewed;         283 AA.
AC   A0QQV6;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=GDP-polyphosphate phosphotransferase {ECO:0000305};
DE            EC=2.7.4.- {ECO:0000269|PubMed:19843229};
DE   AltName: Full=Polyphosphate kinase PPK2 {ECO:0000305};
GN   OrderedLocusNames=MSMEG_0891 {ECO:0000312|EMBL:ABK70472.1};
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19843229; DOI=10.1111/j.1365-2958.2009.06925.x;
RA   Sureka K., Sanyal S., Basu J., Kundu M.;
RT   "Polyphosphate kinase 2: a modulator of nucleoside diphosphate kinase
RT   activity in mycobacteria.";
RL   Mol. Microbiol. 74:1187-1197(2009).
CC   -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC       GDP to GTP. {ECO:0000269|PubMed:19843229}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + GTP = [phosphate](n+1) + GDP;
CC         Xref=Rhea:RHEA:55412, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:19843229};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55414;
CC         Evidence={ECO:0000269|PubMed:19843229};
CC   -!- INDUCTION: Expression increases during the exponential phase of growth
CC       and remains at a steady level up to the stationary phase.
CC       {ECO:0000269|PubMed:19843229}.
CC   -!- DISRUPTION PHENOTYPE: Knockout mutant is more susceptible to acid, heat
CC       and hypoxic stress. Mutant has reduced GTP levels.
CC       {ECO:0000269|PubMed:19843229}.
CC   -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC       I subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000480; ABK70472.1; -; Genomic_DNA.
DR   RefSeq; WP_011727269.1; NZ_SIJM01000010.1.
DR   RefSeq; YP_885294.1; NC_008596.1.
DR   AlphaFoldDB; A0QQV6; -.
DR   SMR; A0QQV6; -.
DR   STRING; 246196.MSMEI_0870; -.
DR   EnsemblBacteria; ABK70472; ABK70472; MSMEG_0891.
DR   GeneID; 66739060; -.
DR   KEGG; msm:MSMEG_0891; -.
DR   PATRIC; fig|246196.19.peg.881; -.
DR   eggNOG; COG2326; Bacteria.
DR   OMA; TKLWFSV; -.
DR   OrthoDB; 953793at2; -.
DR   BRENDA; 2.7.4.34; 3512.
DR   Proteomes; UP000000757; Chromosome.
DR   GO; GO:0008976; F:polyphosphate kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016898; Polyphosphate_phosphotransfera.
DR   InterPro; IPR022488; PPK2-related.
DR   InterPro; IPR022486; PPK2_PA0141.
DR   Pfam; PF03976; PPK2; 1.
DR   PIRSF; PIRSF028756; PPK2_prd; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03707; PPK2_P_aer; 1.
PE   1: Evidence at protein level;
KW   Kinase; Reference proteome; Transferase.
FT   CHAIN           1..283
FT                   /note="GDP-polyphosphate phosphotransferase"
FT                   /id="PRO_0000442585"
SQ   SEQUENCE   283 AA;  33047 MW;  4E20C76E6E08387E CRC64;
     MLDSTGYAVR DDDDDDPELL LPGGEVVDTW REGYPYDERM HRADYEEQKR LLQIELLKLQ
     KWSQAHGHRH VIVFEGRDAA GKGGTIKRFM EHLNPRGARV VALEKPTERE RTQWYFQRYV
     EHLPAAGELV LFDRSWYNRA GVERVMGYCT PKQHAEFIRQ APLFEQMLVN DGISLTKLWF
     SVTRSEQLTR FTIRQVDPVR QWKLSPTDLA SLDKWDDYTA AKEEMFAWTD TEIAPWTVVK
     SNDKKRARIN AMRYVLGKFD YDNKDHEVVG QADPLIVGRA LSD