PK21C_RHIME
ID PK21C_RHIME Reviewed; 284 AA.
AC Q92ZU4;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=ADP-polyphosphate phosphotransferase 3 {ECO:0000305};
DE EC=2.7.4.- {ECO:0000269|PubMed:19001261};
DE AltName: Full=Polyphosphate kinase PPK2 3 {ECO:0000305};
GN ORFNames=SMa0670 {ECO:0000312|EMBL:AAK65012.1};
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; AAK65012.1; -; Genomic_DNA.
DR PIR; B95306; B95306.
DR RefSeq; NP_435600.1; NC_003037.1.
DR RefSeq; WP_010967347.1; NC_003037.1.
DR AlphaFoldDB; Q92ZU4; -.
DR SMR; Q92ZU4; -.
DR EnsemblBacteria; AAK65012; AAK65012; SMa0670.
DR GeneID; 61599179; -.
DR KEGG; sme:SMa0670; -.
DR PATRIC; fig|266834.11.peg.371; -.
DR HOGENOM; CLU_048699_3_0_5; -.
DR OMA; WAPWYVA; -.
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..284
FT /note="ADP-polyphosphate phosphotransferase 3"
FT /id="PRO_0000442591"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 33401 MW; C930DEEFE6C011DE CRC64;
MDKHTDDRKK NNHWKAEDRK SAATEASETR SGGNYAKELA RLQEEIAHLQ AWVKKTGARI
VIVFEGRDAA GKGGVIKRIT ERVSPRVFRV VALPAPTDRE KTQIYMQRYI QQFPAAGEVV
IFDRSWYNRP GVERVMGFCS EKKAKRFLEI APRFEAAMIE SGIVLLKYFL DVSEEEQDRR
FRQRINDPLR QWKLSPMDVE SYRRWWDYTR AYDEMIRMTD TDDAPWWIVP SDNKKQARVN
CIAHILSSIP YERVKFEDPD LGKRQKRPAD FEGDTRRRTV PNLF
