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PK21B_RHIME
ID   PK21B_RHIME             Reviewed;         306 AA.
AC   Q930V2;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=ADP-polyphosphate phosphotransferase 2 {ECO:0000305};
DE            EC=2.7.4.- {ECO:0000269|PubMed:19001261};
DE   AltName: Full=Polyphosphate kinase PPK2 2 {ECO:0000305};
GN   ORFNames=SMa0172 {ECO:0000312|EMBL:AAK64750.1};
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA (megaplasmid 1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA   Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA   Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA   Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA   Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT   meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=19001261; DOI=10.1073/pnas.0807563105;
RA   Nocek B., Kochinyan S., Proudfoot M., Brown G., Evdokimova E., Osipiuk J.,
RA   Edwards A.M., Savchenko A., Joachimiak A., Yakunin A.F.;
RT   "Polyphosphate-dependent synthesis of ATP and ADP by the family-2
RT   polyphosphate kinases in bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:17730-17735(2008).
CC   -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC       ADP to ATP. Can also convert GDP to GTP, with lower efficiency.
CC       {ECO:0000269|PubMed:19001261}.
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;
CC         Evidence={ECO:0000269|PubMed:19001261};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19575;
CC         Evidence={ECO:0000269|PubMed:19001261};
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:19001261};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55414;
CC         Evidence={ECO:0000269|PubMed:19001261};
CC   -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC       I subfamily. {ECO:0000305}.
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DR   EMBL; AE006469; AAK64750.1; -; Genomic_DNA.
DR   PIR; D95273; D95273.
DR   RefSeq; NP_435338.1; NC_003037.1.
DR   RefSeq; WP_010967093.1; NC_003037.1.
DR   AlphaFoldDB; Q930V2; -.
DR   SMR; Q930V2; -.
DR   EnsemblBacteria; AAK64750; AAK64750; SMa0172.
DR   GeneID; 25012243; -.
DR   GeneID; 61598937; -.
DR   KEGG; sme:SMa0172; -.
DR   PATRIC; fig|266834.11.peg.96; -.
DR   HOGENOM; CLU_048699_3_0_5; -.
DR   OMA; NPRICRV; -.
DR   Proteomes; UP000001976; Plasmid pSymA.
DR   GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
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   ATP synthesis; Kinase; Plasmid; Reference proteome; Transferase.
FT   CHAIN           1..306
FT                   /note="ADP-polyphosphate phosphotransferase 2"
FT                   /id="PRO_0000442590"
SQ   SEQUENCE   306 AA;  36371 MW;  E8FB76A566E0C784 CRC64;
     MSNSKDEVER IDWLEAELAD TIDEDYELEL SEPTLSEKIR EIYRKAHPPA LPRMDYFRAL
     LALQAELIKL QDWVVYHKQK VVVIFEGRDA AGKGGVIKRI TQRLNPRIVR TVALPAPSDR
     EKTQWYFQRY VPHLPAGGEI VLFDRSWYNR CGVERVMGFA TEEEVEQFFD DVPEFERMLV
     RSGVRLVKYW FSITDEEQQL RFLTRIHDPL KQWKLSPMDL QSRVRWEAYT KAKEETFART
     NIREAPWHIV EANDKKRARL NCIDHLLKQI PYEDVPHEDI TLPERIFNPN YERKVLPPEL
     YVPAKY
 
 
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