PNP_PASMU
ID PNP_PASMU Reviewed; 714 AA.
AC Q9CLU1; Q9L6A4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=PM1114;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-714.
RX PubMed=10873488; DOI=10.1006/mpat.2000.0365;
RA Fuller T.E., Kennedy M.J., Lowery D.E.;
RT "Identification of Pasteurella multocida virulence genes in a septicemic
RT mouse model using signature-tagged mutagenesis.";
RL Microb. Pathog. 29:25-38(2000).
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: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation.
CC {ECO:0000255|HAMAP-Rule:MF_01595}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR EMBL; AE004439; AAK03198.1; -; Genomic_DNA.
DR EMBL; AF237935; AAF68421.1; -; Genomic_DNA.
DR RefSeq; WP_005723319.1; NC_002663.1.
DR AlphaFoldDB; Q9CLU1; -.
DR SMR; Q9CLU1; -.
DR STRING; 747.DR93_849; -.
DR PRIDE; Q9CLU1; -.
DR EnsemblBacteria; AAK03198; AAK03198; PM1114.
DR KEGG; pmu:PM1114; -.
DR HOGENOM; CLU_004217_2_2_6; -.
DR OMA; LHILDVM; -.
DR Proteomes; UP000000809; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
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; 2.
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 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..714
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329750"
FT DOMAIN 555..614
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 624..692
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 494
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 714 AA; 77011 MW; DB4E3096C9BB1A65 CRC64;
MNPIVKQFKY GQHTVTLETG AIARQATAAV MASMDDTTVF VTVVAKKDVK EGQDFFPLTV
NYQERTYAAG RIPGGFFKRE GRPSEGETLI ARLIDRPIRP LFPEGFYNEI QIVATVVSVN
PQICPDLVAM IGASAALSLS GVPFNGPIGA ARVGFIDDQF VLNPTMNEQK QSRLDLVVAG
TDKAVLMVES EADVLTEEQM LAAVVFGHQQ QQVVIDAIKE FTAEAGKPRW DWVAPEPNTA
LIEKVKAIAE ARLGEAYRIT EKQARYEQID AIKADVIAQI TAEVAEGEDI SEGKIVDIFT
ALESQIVRSR IIAGEPRIDG RTVDTVRALD ICTGVLPRTH GSAIFTRGET QALAVATLGT
ERDAQIIDEL TGERSDHFLF HYNFPPYSVG ETGMIGSPKR REIGHGRLAK RGVAAVMPTL
AEFPYVVRVV SEITESNGSS SMASVCGASL ALMDAGVPIK AAVAGIAMGL VKEDEKFVVL
SDILGDEDHL GDMDFKVAGT RTGVTALQMD IKIEGITAEI MQIALNQAKS ARLHILGVME
QAIPAPRADI SDFAPRIYTM KIDPKKIKDV IGKGGATIRA LTEETGTSID IDDDGTVKIA
AVDGNSAKEV MARIEDITAE VEAGAVYKGK VTRLADFGAF VSIVGNKEGL VHISQIAEER
VEKVSDYLAV GQEVTVKVVE IDRQGRIRLT MKEVAPKQEH VDSVVADVAA EENA
