ID PNP_SALPC Reviewed; 711 AA.
AC C0PZ50;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 01-MAY-2013, entry version 32.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE EC=2.7.7.8;
DE AltName: Full=Polynucleotide phosphorylase;
DE Short=PNPase;
GN Name=pnp; OrderedLocusNames=SPC_3353;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T.,
RA Peng Y.-H., Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R.,
RA Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella
RT choleraesuis and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
CC -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC polyribonucleotides processively in the 3'- to 5'-direction (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside
CC diphosphate.
CC -!- SUBUNIT: Homotrimer. Organized into a structure (processome or RNA
CC degradosome) containing a number of RNA-processing enzymes (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the polyribonucleotide
CC nucleotidyltransferase family.
CC -!- SIMILARITY: Contains 1 KH domain.
CC -!- SIMILARITY: Contains 1 S1 motif domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACN47438.1; Type=Erroneous initiation;
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DR EMBL; CP000857; ACN47438.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_002638879.1; NC_012125.1.
DR ProteinModelPortal; C0PZ50; -.
DR SMR; C0PZ50; 617-692.
DR STRING; 476213.SPC_3353; -.
DR PRIDE; C0PZ50; -.
DR EnsemblBacteria; ACN47438; ACN47438; SPC_3353.
DR GeneID; 7555889; -.
DR KEGG; sei:SPC_3353; -.
DR PATRIC; 32365640; VBISalEnt12305_3413.
DR eggNOG; COG1185; -.
DR HOGENOM; HOG000218326; -.
DR KO; K00962; -.
DR ProtClustDB; PRK11824; -.
DR BioCyc; SENT476213:GH8J-3406-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:HAMAP.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:HAMAP.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.10.10.400; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_01595; PNPase; 1; -.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR009019; KH_prok-type.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012162; PNPase.
DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR022967; RNA-binding_domain_S1.
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; 2.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF46915; 3_ExoRNase; 1.
DR SUPFAM; SSF55666; 3_ExoRNase; 2.
DR SUPFAM; SSF54814; KH_prok; 1.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 2.
DR TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Nucleotidyltransferase; RNA-binding;
KW Transferase.
FT CHAIN 1 711 Polyribonucleotide
FT nucleotidyltransferase.
FT /FTId=PRO_0000381917.
FT DOMAIN 553 612 KH.
FT DOMAIN 622 690 S1 motif.
SQ SEQUENCE 711 AA; 77039 MW; BCF7F15FC536A017 CRC64;
MLNPIVRKFQ YGQHTVTLET GMMARQATAA VMVSMDDTAV FVTVVGQKKA KPGQDFFPLT
VNYQERTYAA GRIPGSFFRR EGRPSEGETL IARLIDRPVR PLFPEGFVNE VQVIATVVSV
NPQVNPDIVA MIGASAALSL SGIPFNGPIG AARVGYINDQ YVLNPTQDEL KESKLDLVVA
GTEAAVLMVE SEAELLSEDT MLGAVVFGHE QQQVVIQAIN DLVKEAGKPR WDWQPEAVND
ALNARVAALA ESRLSDAYRI TDKQERYAQV DVIKSETIEQ LIAEDETLDA NELGEILHAI
EKNVVRSRVL AGEPRIDGRE KDMIRGLDVR TGVLPRTHGS ALFTRGETQA LVTATLGTAR
DAQVLDELMG ERTDSFLFHY NFPPYSVGET GMVGSPKRRE IGHGRLAKRG VLAVMPDMDK
FPYTVRVVSE ITESNGSSSM ASVCGASLAL MDAGVPIKAA VAGIAMGLVK EGDNYVVLSD
ILGDEDHLGD MDFKVAGSRD GISALQMDIK IEGITKEIMQ VALNQAKGAR LHILGVMEQA
INAPRGDISE FAPRIHTIKI STDKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVKIAAT
DGEKAKYAIR RIEEITAEIE VGRIYNGKVT RIVDFGAFVA IGGGKEGLVH ISQIADKRVE
KVTDYLQMGQ EVPVKVLEVD RQGRVRLSIK EATEQSQPAA APEAPASEQA E
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