ID A0A0S2DGA3_LYSEN Unreviewed; 702 AA.
AC A0A0S2DGA3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01595};
DE EC=2.7.7.8 {ECO:0000256|HAMAP-Rule:MF_01595};
DE AltName: Full=Polynucleotide phosphorylase {ECO:0000256|HAMAP-Rule:MF_01595};
DE Short=PNPase {ECO:0000256|HAMAP-Rule:MF_01595};
GN Name=pnp {ECO:0000256|HAMAP-Rule:MF_01595,
GN ECO:0000313|EMBL:QCW26120.1};
GN ORFNames=BV903_015705 {ECO:0000313|EMBL:UZW58756.1}, FE772_11000
GN {ECO:0000313|EMBL:QCW26120.1}, GLE_2180 {ECO:0000313|EMBL:ALN57529.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN57529.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN57529.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN57529.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UZW58756.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B25 {ECO:0000313|EMBL:UZW58756.1};
RX PubMed=28473380; DOI=10.1128/genomea.00271-17;
RA Hernandez I., Fernandez C.;
RT "Draft Genome Sequence and Assembly of a Lysobacter enzymogenes Strain with
RT Biological Control Activity against Root Knot Nematodes.";
RL Genome Announc. 5:e00271-e00217(2017).
RN [3] {ECO:0000313|EMBL:QCW26120.1, ECO:0000313|Proteomes:UP000308311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC36 {ECO:0000313|EMBL:QCW26120.1,
RC ECO:0000313|Proteomes:UP000308311};
RA Feng T.;
RT "Intraspecies Signal LeDSF and Interspecies Signal Indole Synergistically
RT Regulate the Twitching Motility of Lysobacter enzymogenes.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:UZW58756.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B25 {ECO:0000313|EMBL:UZW58756.1};
RA Fernandez G., Fernandez C., Hernandez I.;
RT "Improved assembly of Lysobacter enzymogenes B25.";
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of
CC single-stranded polyribonucleotides processively in the 3'- to 5'-
CC direction. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01595}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404, ECO:0000256|HAMAP-
CC Rule:MF_01595}.
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DR EMBL; CP013140; ALN57529.1; -; Genomic_DNA.
DR EMBL; CP040656; QCW26120.1; -; Genomic_DNA.
DR EMBL; CP110813; UZW58756.1; -; Genomic_DNA.
DR RefSeq; WP_057947343.1; NZ_CP110813.1.
DR STRING; 69.GLE_2180; -.
DR KEGG; lez:GLE_2180; -.
DR PATRIC; fig|69.6.peg.2142; -.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000061569; Chromosome.
DR Proteomes; UP000190203; Chromosome.
DR Proteomes; UP000308311; 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 CDD; cd02393; KH-I_PNPase; 1.
DR CDD; cd11363; RNase_PH_PNPase_1; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 1.
DR CDD; cd04472; S1_PNPase; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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_Su5_D2-typ_SF.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR03591; polynuc_phos; 1.
DR PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 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; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 1.
DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01595};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01595};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01595};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01595}; Reference proteome {ECO:0000313|Proteomes:UP000061569};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01595};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01595}.
FT DOMAIN 623..691
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ SEQUENCE 702 AA; 75322 MW; 9A2973AB982B2798 CRC64;
MAKITKTFQY GNHQVTLETG EIARQAGGAV IVKMDDTVLL VTAVAAKSAR EGQDFFPLTV
DYQEKFYAGG RIPGGFFKRE GRATEKETLI SRLIDRPIRP LFPEDYRNEV QIIATVMSLN
PEVDGDIPAL IGASAAMALA GTPFQGPIGA AKVGYKNGQY LLNPTAAELA DSDLELVVAG
TSNAVLMVES EANMLSEEVM LGAVMFGHRE MQKVINVINE LVVEAGTKPS SWEAPAKNEA
LIGALKEAVG DQLAGAFQVR DKLQRRDAIG AIKKDVLLSL AGRAESEGWS SGELSKEFGE
LEYQTMRSSV LDTKIRIDGR ALDTVRPISS KVGVLPRTHG SSLFTRGETQ AIVVATLGTA
RDGQIIDAVS GEYKEHFLFH YNFPPFSVGE CGRMMGPKRR EIGHGRLAKR GVLAVMPSME
AFPYTIRVVS EITESNGSSS MASVCGSSLA LMDAGVPIKA PVAGIAMGLV KEGDNFVVLS
DILGDEDHLG DMDFKVAGTS EGISALQMDI KIQGITEEIM KVALEQAKAG RLHILGEMAH
AITESRSELS EYAPRLLTMK IHPDKIREVI GKGGSTIQAI TKETGTQIDI QDDGTIVIAS
VNAAAAQAAK SRIDQIVSDV EPGRIYEGKV AKIMDFGAFV TILPGKDGLV HVSQISSERV
EKVSDKLKEG DVVKVKVLEV DKQGRIRLSI KAVEEGEGVS AE
//
