PNP_STAA8
ID PNP_STAA8 Reviewed; 698 AA.
AC Q2FZ20;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, 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}; Synonyms=pnpA;
GN OrderedLocusNames=SAOUHSC_01251;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP INTERACTION WITH ENO AND RNJA, AND SUBUNIT.
RC STRAIN=UAMS-1;
RX PubMed=21764917; DOI=10.1128/jb.05485-11;
RA Roux C.M., DeMuth J.P., Dunman P.M.;
RT "Characterization of components of the Staphylococcus aureus mRNA
RT degradosome holoenzyme-like complex.";
RL J. Bacteriol. 193:5520-5526(2011).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=SA564;
RX PubMed=22447609; DOI=10.1128/aem.00202-12;
RA Redder P., Linder P.;
RT "New range of vectors with a stringent 5-fluoroorotic acid-based
RT counterselection system for generating mutants by allelic replacement in
RT Staphylococcus aureus.";
RL Appl. Environ. Microbiol. 78:3846-3854(2012).
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: Homodimer (Probable). Component of a possible RNA degradosome
CC complex composed of cshA, eno, pfkA, pnp, rnjA, rnjB, rnpA and rny.
CC Interacts specifically RNA helicase CshA and RNase J1.
CC {ECO:0000269|PubMed:21764917, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:22447609}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR EMBL; CP000253; ABD30352.1; -; Genomic_DNA.
DR RefSeq; WP_000076690.1; NZ_LS483365.1.
DR RefSeq; YP_499784.1; NC_007795.1.
DR PDB; 5XEX; X-ray; 2.20 A; A/B/C/D/E/F=1-553.
DR PDBsum; 5XEX; -.
DR AlphaFoldDB; Q2FZ20; -.
DR SMR; Q2FZ20; -.
DR STRING; 1280.SAXN108_1278; -.
DR EnsemblBacteria; ABD30352; ABD30352; SAOUHSC_01251.
DR GeneID; 3919982; -.
DR KEGG; sao:SAOUHSC_01251; -.
DR PATRIC; fig|93061.5.peg.1145; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_9; -.
DR OMA; LHILDVM; -.
DR PRO; PR:Q2FZ20; -.
DR Proteomes; UP000008816; 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..698
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000260060"
FT DOMAIN 557..616
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 626..694
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 183..196
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 198..226
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 292..316
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 338..349
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 352..361
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 402..416
FT /evidence="ECO:0007829|PDB:5XEX"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 428..437
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 442..456
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 466..474
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 479..484
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 487..492
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 493..501
FT /evidence="ECO:0007829|PDB:5XEX"
FT STRAND 506..516
FT /evidence="ECO:0007829|PDB:5XEX"
FT HELIX 520..544
FT /evidence="ECO:0007829|PDB:5XEX"
SQ SEQUENCE 698 AA; 77362 MW; 6EABFB86EDFBFB2E CRC64;
MSQEKKVFKT EWAGRSLTIE TGQLAKQANG AVLVRYGDTV VLSTATASKE PRDGDFFPLT
VNYEEKMYAA GKIPGGFKKR EGRPGDDATL TARLIDRPIR PLFPKGYKHD VQIMNMVLSA
DPDCSPQMAA MIGSSMALSV SDIPFQGPIA GVNVGYIDGK YIINPTVEEK EVSRLDLEVA
GHKDAVNMVE AGASEITEQE MLEAIFFGHE EIQRLVDFQQ QIVDHIQPVK QEFIPAERDE
ALVERVKSLT EEKGLKETVL TFDKQQRDEN LDNLKEEIVN EFIDEEDPEN ELLIKEVYAI
LNELVKEEVR RLIADEKIRP DGRKPDEIRP LDSEVGILPR THGSGLFTRG QTQALSVLTL
GALGDYQLID GLGPEEEKRF MHHYNFPNFS VGETGPVRAP GRREIGHGAL GERALKYIIP
DTADFPYTIR IVSEVLESNG SSSQASICGS TLALMDAGVP IKAPVAGIAM GLVTREDSYT
ILTDIQGMED ALGDMDFKVA GTKEGITAIQ MDIKIDGLTR EIIEEALEQA RRGRLEIMNH
MLQTIDQPRT ELSAYAPKVV TMTIKPDKIR DVIGPGGKKI NEIIDETGVK LDIEQDGTIF
IGAVDQAMIN RAREIIEEIT REAEVGQTYQ ATVKRIEKYG AFVGLFPGKD ALLHISQISK
NRIEKVEDVL KIGDTIEVKI TEIDKQGRVN ASHRALEE
