PNP_ACIBS
ID PNP_ACIBS Reviewed; 697 AA.
AC B0VLR7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=ABSDF3154;
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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; CU468230; CAP02433.1; -; Genomic_DNA.
DR PDB; 6D6K; X-ray; 2.50 A; A/B=1-697.
DR PDBsum; 6D6K; -.
DR AlphaFoldDB; B0VLR7; -.
DR SMR; B0VLR7; -.
DR EnsemblBacteria; CAP02433; CAP02433; ABSDF3154.
DR KEGG; abm:ABSDF3154; -.
DR HOGENOM; CLU_004217_2_2_6; -.
DR OMA; LHILDVM; -.
DR Proteomes; UP000001741; 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 RNA-binding; Transferase.
FT CHAIN 1..697
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_1000147874"
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 7..13
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:6D6K"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 264..281
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 293..312
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 336..347
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 350..359
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 372..383
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 400..414
FT /evidence="ECO:0007829|PDB:6D6K"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 426..435
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 440..455
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 464..473
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 476..482
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 485..490
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 492..499
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 504..511
FT /evidence="ECO:0007829|PDB:6D6K"
FT HELIX 518..540
FT /evidence="ECO:0007829|PDB:6D6K"
FT STRAND 559..563
FT /evidence="ECO:0007829|PDB:6D6K"
SQ SEQUENCE 697 AA; 75262 MW; 89CD7BD2531FB517 CRC64;
MSMFNIVRKE FQFGQHQVVL ETGRVARQAN TVLITMGGVT VLVAVVAAPT AKAGQDFFPL
TVNYQEKQYA AGRIPGGYGK REGRASEAET LTSRLIDRPI RPLFPEGYYN EIQVTATVVS
SDKTMEADIA AMLGTSAALA IAGTPFRGPI GAARVGLING EYVLNPNFEQ MAQSDLDLVV
AGTESAVLMV ESEAKELSED QMLGAVLFGH DEMQIAIQAI NEFAAAAGAK PSDWVAPAHN
EELRAKLKEA FEAKISEAYT IAVKQDRYAA LDALHAEAVA QFVPEEDVDG IADEVDYLFE
DLKYRTVRDN ILSGKPRIDG RDTKTVRALD VQVGVLERAH GSALFTRGET QALVTTTLGN
TRDALMVDTL AGTKTDNFML HYNFPAYSVG ETGRESGPKR REIGHGRLAR RGVQAVLPAA
DRFPYVIRIV SDITESNGSS SMASVCGASL SLMDAGVPLK APVAGIAMGL VKEGERFAVL
SDILGDEDHL GDMDFKVAGS ANGITALQMD IKIEGITEEI MEVALNQAFA GRMHILNEMN
KVISRARPEI SMHAPTFEVI TINPDKIRDV IGKGGATIRQ ITEETKAAID IEDNGTVRVF
GETKAAAKAA IAKIQAITAE VEPGKIYDGK VIRIVEFGAF VNIMPGTDGL LHISQISNER
ITNVTDVLKE GQEVKVQVQD VDNRGRIKLT MKDIEQA
