ID PNP_CAUVC Reviewed; 712 AA.
AC Q9AC32;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 114.
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=CC_0034;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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 -!- 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; AE005673; AAK22022.1; -; Genomic_DNA.
DR PIR; B87253; B87253.
DR RefSeq; NP_418854.1; NC_002696.2.
DR RefSeq; WP_010917924.1; NC_002696.2.
DR PDB; 4AID; X-ray; 2.60 A; A/B/C=1-712.
DR PDB; 4AIM; X-ray; 3.30 A; A=1-712.
DR PDB; 4AM3; X-ray; 3.00 A; A/B/C=1-712.
DR PDBsum; 4AID; -.
DR PDBsum; 4AIM; -.
DR PDBsum; 4AM3; -.
DR AlphaFoldDB; Q9AC32; -.
DR SMR; Q9AC32; -.
DR STRING; 190650.CC_0034; -.
DR EnsemblBacteria; AAK22022; AAK22022; CC_0034.
DR KEGG; ccr:CC_0034; -.
DR PATRIC; fig|190650.5.peg.34; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_5; -.
DR BioCyc; CAULO:CC0034-MONOMER; -.
DR Proteomes; UP000001816; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..712
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329577"
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"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4AM3"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 186..196
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 239..258
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:4AID"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 295..312
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 339..347
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 350..359
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 400..413
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:4AID"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 426..435
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 440..454
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 464..472
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 487..490
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 491..500
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 503..511
FT /evidence="ECO:0007829|PDB:4AID"
FT HELIX 518..540
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:4AIM"
FT STRAND 556..561
FT /evidence="ECO:0007829|PDB:4AM3"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:4AM3"
FT HELIX 567..571
FT /evidence="ECO:0007829|PDB:4AM3"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:4AM3"
FT HELIX 576..585
FT /evidence="ECO:0007829|PDB:4AM3"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:4AM3"
FT STRAND 593..603
FT /evidence="ECO:0007829|PDB:4AM3"
FT HELIX 604..612
FT /evidence="ECO:0007829|PDB:4AID"
FT STRAND 627..635
FT /evidence="ECO:0007829|PDB:4AIM"
FT STRAND 638..646
FT /evidence="ECO:0007829|PDB:4AIM"
FT STRAND 649..659
FT /evidence="ECO:0007829|PDB:4AIM"
FT TURN 662..664
FT /evidence="ECO:0007829|PDB:4AIM"
FT STRAND 673..680
FT /evidence="ECO:0007829|PDB:4AIM"
FT TURN 683..685
FT /evidence="ECO:0007829|PDB:4AIM"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:4AIM"
SQ SEQUENCE 712 AA; 76448 MW; 4772C4229037CA96 CRC64;
MFDIKRKTIE WGGKTLVLET GRIARQADGA VLATMGETVV LATAVFAKSQ KPGQDFFPLT
VNYQEKTFAA GKIPGGFFKR EGRPSEKETL VSRLIDRPIR PLFVKGFKNE VQVVVTVLQH
DLENDPDILG MVAASAALCL SGAPFMGPIG AARVGWVDGA YVLNPTLDEM KESKMDLVVA
GTADAVMMVE SEIQELSEEI VLGGVNFAHQ QMQAVIDAII DLAEHAAKEP FAFEPEDTDA
IKAKMKDLVG ADIAAAYKIQ KKQDRYEAVG AAKKKAIAAL GLSDENPTGY DPLKLGAIFK
ELEADVVRRG ILDTGLRIDG RDVKTVRPIL GEVGILPRTH GSALFTRGET QAIVVATLGT
GDDEQFIDAL EGTYKESFLL HYNFPPYSVG ETGRMGSPGR REIGHGKLAW RALRPMLPTK
EDFPYTIRLV SEITESNGSS SMATVCGSSL AMMDAGVPLV RPVSGIAMGL ILEQDGFAVL
SDILGDEDHL GDMDFKVAGT SEGLTSLQMD IKIAGITPAI MEQALAQAKE GRAHILGEMN
KAMDAPRADV GDFAPKIETI NIPTDKIREV IGSGGKVIRE IVATTGAKVD INDDGVVKVS
ASDGAKIKAA IDWIKSITDE AEVGKIYDGK VVKVVDFGAF VNFFGAKDGL VHVSQISNER
VAKPSDVLKE GQMVKVKLLG FDDRGKTKLS MKVVDQETGE DLSKKEAAAE EA
//
