PNP_PHOLU
ID PNP_PHOLU Reviewed; 709 AA.
AC P41121;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
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}; Synonyms=pph;
OS Photorhabdus luminescens (Xenorhabdus luminescens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=29488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-13.
RC STRAIN=K122;
RX PubMed=8206856; DOI=10.1128/jb.176.12.3775-3784.1994;
RA Clarke D.J., Dowds B.C.A.;
RT "The gene coding for polynucleotide phosphorylase in Photorhabdus sp.
RT strain K122 is induced at low temperatures.";
RL J. Bacteriol. 176:3775-3784(1994).
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.
CC -!- INDUCTION: In response to low temperature.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR EMBL; X76069; CAA53671.1; -; Genomic_DNA.
DR PIR; S38883; S38883.
DR AlphaFoldDB; P41121; -.
DR SMR; P41121; -.
DR STRING; 29488.KS18_11530; -.
DR PRIDE; P41121; -.
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; IPR036456; PNPase_PH_RNA-bd_sf.
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; SSF46915; SSF46915; 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; Direct protein sequencing; Magnesium; Metal-binding;
KW Nucleotidyltransferase; RNA-binding; Stress response; Transferase.
FT CHAIN 1..709
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000197915"
FT DOMAIN 553..612
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 622..690
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 709 AA; 76745 MW; EBFCC559FC921E6B CRC64;
MLNPIVRKFQ YGQHTVTIET GMMARQATAA VMVNMDDTAV FVTVVGQKKV KAGQDFFPLT
VNYQERTYAA GRIPGSFFRR EGRPGEGETL VARLIDRPLR PLFPEGFLNE VRIVATVVSV
NPQINPDIVA MIGASAALAL SGIPFNGPIG AARVGYINDQ YVLNPTSDEL KNSRLDLVVS
GTAGAVLMVE SEADLLTEEQ MLGAVVFGHD QQQVVIDNIN ALAAEAGKEK WDWVPEPVNQ
ALHDRVAELA ESRLGDAYRI TEKQERYAQV DAIKDEVTAA LLEQDETLEE AEIHEILGSL
EKNVVRSRVL SGEPRIDGRE KDMVRALDVR TGVLPRTHGS ALFTRGETQA LVTATLGTER
DAQIIDELMG ERTDRFLLHY NFPPYSVGET GMMGSPKRRE IGHGRLAKRG VLAVMPKANE
FPYTVRVVSE ITESNGSSSM ASVCGASLAL MDAGVPIKAA VAGIAMGLVK EGDNFVVLSD
ILGDEDHLGD MDFKVAGSCE GISALQMDIK IEGITREIMQ VALNQAKGAR LHILSVMEQA
ITTPRDDISQ FAPRIHTIKI NPDKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVKIAAT
DGEKAKHAIS RIEEITAEIE VGRIYAGKVT RIVDFGAFVA IGGGKEGLVH ISQIADKRVE
KVADYLQVGQ ETSVKVLEID RQGRVRLSIK EATAGTAVEE APPAPQSAE
