PNP_COXBU
ID PNP_COXBU Reviewed; 696 AA.
AC Q83D87;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=CBU_0852;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90386.1; -; Genomic_DNA.
DR RefSeq; NP_819872.1; NC_002971.3.
DR RefSeq; WP_010957848.1; NC_002971.4.
DR PDB; 4NBQ; X-ray; 2.91 A; A/B/C=1-696.
DR PDBsum; 4NBQ; -.
DR AlphaFoldDB; Q83D87; -.
DR SMR; Q83D87; -.
DR STRING; 227377.CBU_0852; -.
DR PRIDE; Q83D87; -.
DR DNASU; 1208745; -.
DR EnsemblBacteria; AAO90386; AAO90386; CBU_0852.
DR GeneID; 1208745; -.
DR KEGG; cbu:CBU_0852; -.
DR PATRIC; fig|227377.7.peg.837; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_6; -.
DR OMA; LHILDVM; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
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; 2.
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 3D-structure; Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..696
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329612"
FT DOMAIN 556..615
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 625..693
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 185..195
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 239..256
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 262..284
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 294..313
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 351..360
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 374..384
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 401..414
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:4NBQ"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 427..436
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 441..455
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 465..474
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:4NBQ"
FT TURN 487..491
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 492..500
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 505..512
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 519..543
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 557..562
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 568..572
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 577..586
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:4NBQ"
FT STRAND 594..604
FT /evidence="ECO:0007829|PDB:4NBQ"
FT HELIX 605..619
FT /evidence="ECO:0007829|PDB:4NBQ"
FT TURN 655..657
FT /evidence="ECO:0007829|PDB:4NBQ"
SQ SEQUENCE 696 AA; 76331 MW; 9E55E7C7CD00E52B CRC64;
MNKIRKTFQY GKHEVTFETG EMARQATGAV VVRMGDTVLL VSVVAKKEAE EGRDFFPLTV
NYQEKTYAAG KIPGGYFKRE GRPTEKETLT SRLIDRPLRP LFPKGFTNEV QVIATVLSVD
SKVPTDIPAI LGASAAIGLS GIPFNGSLGA ARVGYRGGEY LLNPSLDELK DSALDLVVAG
TRDAVLMVES EAQELPESVM LGAVLHGHQA MQVAIQAIAE FIQEAGGAKW EWEPPTVNTA
LEKWVVEKSE APLKKAYQIQ EKTARQAQIQ AIRDQLLADR AAEREGEENA VNEHELAVIF
HELERRIVRE QILTGQPRID GRDTKTVRPI TVKVGVLPRS HGSALFTRGE TQALVVTTLG
TERDAQSIDD LDGDRQEEFI FHYNFPPFCV GEVGFMSGPK RREIGHGRLA KRAVVPVVPT
LDKFPYVIRV VSEILESNGS SSMASVCGSS LALMDAGVPT KAPVAGIAMG LIKENDKYAV
LSDILGDEDH LGDMDFKVAG TSNGVTALQM DIKIEGITKE IMEQALDQAK EGRLHILSIM
NKVLDKPRSQ VSDLAPQYVT MKINPEKIRD VIGKGGVVIR EITEATNCAI DISDDGTIKI
AAHTTEEGEA AKRRIEELTA EVELGKVYEG TVVKITDFGA FVQILPNTQG LVHISQIAQE
RVENVRDYLE EGQVIRVKVI EIDRQGRVRL SMKQID
