PNP_SYNY3
ID PNP_SYNY3 Reviewed; 718 AA.
AC P72659;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595};
DE EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595};
DE AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595};
DE Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595};
GN Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595}; OrderedLocusNames=sll1043;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=12601000; DOI=10.1074/jbc.m211571200;
RA Rott R., Zipor G., Portnoy V., Liveanu V., Schuster G.;
RT "RNA polyadenylation and degradation in cyanobacteria are similar to the
RT chloroplast but different from Escherichia coli.";
RL J. Biol. Chem. 278:15771-15777(2003).
RN [3]
RP SUBUNIT.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=24563514; DOI=10.1261/rna.043513.113;
RA Zhang J.Y., Deng X.M., Li F.P., Wang L., Huang Q.Y., Zhang C.C., Chen W.L.;
RT "RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria
RT via a cyanobacterial-specific nonapeptide in the noncatalytic region.";
RL RNA 20:568-579(2014).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=27215789; DOI=10.1128/jb.00267-16;
RA Rosana A.R., Whitford D.S., Fahlman R.P., Owttrim G.W.;
RT "Cyanobacterial RNA Helicase CrhR Localizes to the Thylakoid Membrane
RT Region and Cosediments with Degradosome and Polysome Complexes in
RT Synechocystis sp. Strain PCC 6803.";
RL J. Bacteriol. 198:2089-2099(2016).
CC -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of
CC single-stranded polyribonucleotides processively in the 3'- to 5'-
CC direction. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC -!- SUBUNIT: Interacts with RNase E (rne). {ECO:0000269|PubMed:24563514}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC Note=Some of the protein cosediments with polysomes.
CC {ECO:0000269|PubMed:27215789}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:12601000}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR EMBL; BA000022; BAA16661.1; -; Genomic_DNA.
DR PIR; S74509; S74509.
DR AlphaFoldDB; P72659; -.
DR SMR; P72659; -.
DR IntAct; P72659; 3.
DR STRING; 1148.1651733; -.
DR PaxDb; P72659; -.
DR EnsemblBacteria; BAA16661; BAA16661; BAA16661.
DR KEGG; syn:sll1043; -.
DR eggNOG; COG1185; Bacteria.
DR InParanoid; P72659; -.
DR OMA; LHILDVM; -.
DR PhylomeDB; P72659; -.
DR BRENDA; 2.7.7.8; 382.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR Gene3D; 3.30.230.70; -; 2.
DR HAMAP; MF_01595; PNPase; 1.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012162; PNPase.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR11252; PTHR11252; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF03726; PNPase; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 1.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF55666; SSF55666; 2.
DR TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..718
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329905"
FT DOMAIN 564..623
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 633..701
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 718 AA; 77831 MW; 138A985B4AC76FEB CRC64;
MQEFDKSISF DGRDIRLKMG TLAPQAGGSV LIQSGDTAVL VTATRAKGRD GIDFLPLTVD
YEGRLYAAGR IPGGFLRREG RPPEKATLIS RLIDRPLRPL FPHWLRDELQ IVATTLSMDE
EVPPDVLAVT GASVAVILAQ IPFKGPMAAV RVGLVGDDFI INPTYREVHN GDLDLVVAGT
PAGIVMVEAG ANQLPEQDII EAIDFGYEAV QDLINAQREL MTDLGITLAT SEPPPVNTAV
EEFIANRASK KIITVLGQFD LGKDGRDAAL DEIKATEVET AIAELPETDP VKQSVEEDPK
LVGNLYKALT KKLMRKQIVD DGVRVDGRKL EQVRPISCEV GFLPRRVHGS GLFNRGLTQV
LSLATLGSPG DAQDLADDLH PEDEKRYLHH YNFPPYSVGE ARPMRSPGRR EIGHGALAER
AIIPVLPPQE DFPYVVRVVS EVLSSNGSTS MGSVCGSTLA LMDAGVPIKK PVSGAAMGLI
KEGDEIRILT DIQGIEDFLG DMDFKVAGTD SGITALQMDM KIDGLSMEVV SKAIMQALPA
RLHILDKMLA TIREPRPELS PFAPRLLTLK IEPEHIGMVI GPGGKTIKGI TEQTSCKIDI
ADDGTVTIAS SEGERAERAR QMIYNMTRKL NEGEVYLGRV TRIIPIGAFV EVLPGKEGMI
HISQLTEGRV GKVEDEVGVG DEVIVKVREI DSKGRLNLTR LGIHPDEAAE ARRNASRG
