PNP_BIFLS
ID PNP_BIFLS Reviewed; 914 AA.
AC B7GNH2; E8MNQ3;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
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};
GN OrderedLocusNames=Blon_2270, BLIJ_2342;
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=391904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001095; ACJ53328.1; -; Genomic_DNA.
DR EMBL; AP010889; BAJ69919.1; -; Genomic_DNA.
DR RefSeq; WP_012578501.1; NC_017219.1.
DR AlphaFoldDB; B7GNH2; -.
DR SMR; B7GNH2; -.
DR PRIDE; B7GNH2; -.
DR EnsemblBacteria; ACJ53328; ACJ53328; Blon_2270.
DR KEGG; bln:Blon_2270; -.
DR KEGG; blon:BLIJ_2342; -.
DR PATRIC; fig|391904.8.peg.2345; -.
DR HOGENOM; CLU_004217_1_0_11; -.
DR OMA; LHILDVM; -.
DR Proteomes; UP000001360; 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; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR014069; GPSI/PNP.
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; PF00575; S1; 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 TIGRFAMs; TIGR02696; pppGpp_PNP; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase; RNA-binding;
KW Transferase.
FT CHAIN 1..914
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000381867"
FT DOMAIN 587..646
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 658..730
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 407..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 527
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 914 AA; 101922 MW; 24F9B6F629FCA9E1 CRC64;
MEGPEIKAVE AVIDNGSFGK RTLRFETGRL AQQADGAVAA YLDDDSMILS TTTAGSSPKE
NYDFFPLTVD VEEKMYAAGK IPGSFFRREG RPSSEAILAC RIIDRPLRPL FPHTLRNEVQ
VVETVLAVNP DDAYDVIALN AASASTMISG LPFEGPVSGV RLALIDGQWV AFPRWSERER
AVFEIVVAGR VVENGDVAIA MIEAGAGKNA WHLIYDEGQT KPDEEVVAGG LEAAKPFIKV
ICEAQDELKK IAAKETKEFQ LFPEYTDELY ARIDEIAHKD LDEALSIAEK LPRQDRIHEI
KEHVREVLAD EFTDMDDAEK DKELGNAFKE LQRQIVRRRI LTEDYRIDGR GLRDIRTLSA
EVDIVPRVHG SALFQRGETQ ILGVTTLNML KMEQQIDALS GPQSKRYMHN YEMPPYSTGE
TGRVGSPKRR EIGHGALAEK ALVPVLPSRE EFPYAIRQVS EAIGSNGSTS MGSVCASTLS
LLAAGVPLKA PVAGIAMGLV SGDVDGQHIF KTLTDILGAE DAFGDMDFKV AGTSEFITAL
QLDTKLDGIP ADILAAALQQ AKEARATILE VINECIDGPA EMSEFAPRII TTSVPVEKIG
EVIGPKGKMI NQIQEDTGAE IAIEDDGTVF ISSEGGEAAK KAKSIIDSIA NPHVPEAGET
YNGKVVKTTS FGAFVNLTPG TDGLLHISQI RNLANGERID AVEDVLREGD TVEVIVQGVD
DRGKISLAIP GFEDQENNAR PSRGDRDDRR GGRGRGDRDD RRGGRGRRSD RDDRDFDDRD
DRPRRRRSDD FEDDYDDRPR RRRSDDRDFD RDDRDDDRPR RRRSADRDFD DRDDRDARDS
RDDDRPRRRR SADRDDRGDR DDRRGGFRGG RGRGSDRNPR YATDDNYDDY RADREERTER
PRRRVRRDFD PFED
