PNP_STRMU
ID PNP_STRMU Reviewed; 730 AA.
AC Q8DWB2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=SMU_155;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN57931.1; -; Genomic_DNA.
DR RefSeq; NP_720625.1; NC_004350.2.
DR RefSeq; WP_002263007.1; NC_004350.2.
DR PDB; 3H36; X-ray; 1.80 A; A=231-320.
DR PDBsum; 3H36; -.
DR AlphaFoldDB; Q8DWB2; -.
DR SMR; Q8DWB2; -.
DR STRING; 210007.SMU_155; -.
DR PRIDE; Q8DWB2; -.
DR EnsemblBacteria; AAN57931; AAN57931; SMU_155.
DR KEGG; smu:SMU_155; -.
DR PATRIC; fig|210007.7.peg.132; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_9; -.
DR OMA; LHILDVM; -.
DR PhylomeDB; Q8DWB2; -.
DR EvolutionaryTrace; Q8DWB2; -.
DR Proteomes; UP000002512; 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; 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..730
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329868"
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 REGION 691..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 HELIX 238..257
FT /evidence="ECO:0007829|PDB:3H36"
FT HELIX 261..283
FT /evidence="ECO:0007829|PDB:3H36"
FT HELIX 289..311
FT /evidence="ECO:0007829|PDB:3H36"
SQ SEQUENCE 730 AA; 80055 MW; DF9A8A2DBA25703F CRC64;
MSKQVFETIF AGKKLAVEIG QVAKQANGAA LVRYGDSTVL SAAVMSKKMS TGDFFPLQIN
YEEKRYAAGK FPGGFNKREG RPSTDATLTA RLIDRPIRPM FAEGFRNEVQ VINTVLSYDA
DASAPMAAMF GSSLALSISD IPFNGPIAGV QVAYLDGQYV INPTAEEKKA SLLELTVAGT
KEAINMVESG AKELSEDIML EALLKGHEAV RELIAFQEEI IAAVGKEKAE VELLQVDADL
QAEIVGKYNA DLQKAVQIEE KKAREIATEA VKEHVTAEYE ERYAEHEEHD RIMRDVAEIL
EQMEHAEVRR LITEDKVRPD GRRVDEIRPL DAEIDFLPKV HGSGLFTRGQ TQALSVLTLA
PMGDTQIVDG LDEEYKKRFM HHYNFPQYSV GETGRYGAPG RREIGHGALG ERALAQVLPS
LEAFPYAIRL VAEVLESNGS SSQASICAGT LALMAGGVPI KAPVAGIAMG LISDGTNYTV
LTDIQGLEDH FGDMDFKVAG TREGITALQM DIKIEGITPQ ILEEALAQAK KARFEILDVI
EKVIPAPRLE LAPTAPKIDT IKVDVDKIKI VIGKGGETID KIIEETGVKI DIDEDGNIAI
YSSDQEAINR TKEIIASLVR EAKVGEIYEA EVVRIEKFGA FVHLFDKTDA LVHISEIAWT
RTNKVEDVLA VGDKVTVKVV KVDDKGRIDA SMKALLPRPP RSEKSNKEDH QSVRHHGSPK
DDKGKEKYDK
