ORN_ECOLI
ID ORN_ECOLI Reviewed; 181 AA.
AC P0A784; P39287; P76799; Q2M6E0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Oligoribonuclease;
DE EC=3.1.15.-;
GN Name=orn; Synonyms=o204a, yjeR; OrderedLocusNames=b4162, JW5740;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-14, POSSIBLE SUBUNIT, AND FUNCTION.
RX PubMed=9573169; DOI=10.1128/jb.180.10.2779-2781.1998;
RA Zhang X., Zhu L., Deutscher M.P.;
RT "Oligoribonuclease is encoded by a highly conserved gene in the 3'-5'
RT exonuclease superfamily.";
RL J. Bacteriol. 180:2779-2781(1998).
RN [5]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=7608090; DOI=10.1128/jb.177.14.4137-4139.1995;
RA Yu D., Deutscher M.P.;
RT "Oligoribonuclease is distinct from the other known exoribonucleases of
RT Escherichia coli.";
RL J. Bacteriol. 177:4137-4139(1995).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=10200269; DOI=10.1073/pnas.96.8.4372;
RA Ghosh S., Deutscher M.P.;
RT "Oligoribonuclease is an essential component of the mRNA decay pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4372-4377(1999).
RN [7]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=16682444; DOI=10.1093/nar/gkl247;
RA Mechold U., Ogryzko V., Ngo S., Danchin A.;
RT "Oligoribonuclease is a common downstream target of lithium-induced pAp
RT accumulation in Escherichia coli and human cells.";
RL Nucleic Acids Res. 34:2364-2373(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-181, AND SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15039570; DOI=10.1107/s0907444904002252;
RA Fiedler T.J., Vincent H.A., Zuo Y., Gavrialov O., Malhotra A.;
RT "Purification and crystallization of Escherichia coli oligoribonuclease.";
RL Acta Crystallogr. D 60:736-739(2004).
CC -!- FUNCTION: 3'-to-5' exoribonuclease specific for small
CC oligoribonucleotides 2 to 5 nucleotides in length, as well as small (2
CC to 5 nucleotides) ssDNA oligomers. Probably responsible for the final
CC step in mRNA degradation. {ECO:0000269|PubMed:16682444,
CC ECO:0000269|PubMed:7608090, ECO:0000269|PubMed:9573169}.
CC -!- ACTIVITY REGULATION: Inhibited by adenosine 3',5'-bisphosphate (PAP).
CC {ECO:0000269|PubMed:16682444}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15039570}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Essential. In depletion experiments the level of
CC oligonucleotides is elevated and that of mononucleotides is severely
CC reduced compared to wild-type. {ECO:0000269|PubMed:10200269}.
CC -!- SIMILARITY: Belongs to the oligoribonuclease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97061.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97061.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77122.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78166.1; -; Genomic_DNA.
DR PIR; S56390; S56390.
DR RefSeq; NP_418586.4; NC_000913.3.
DR RefSeq; WP_001295188.1; NZ_STEB01000014.1.
DR PDB; 1YTA; X-ray; 2.20 A; A/B/C/D=2-181.
DR PDB; 2IGI; X-ray; 1.70 A; A/B=2-181.
DR PDBsum; 1YTA; -.
DR PDBsum; 2IGI; -.
DR AlphaFoldDB; P0A784; -.
DR SMR; P0A784; -.
DR BioGRID; 4261079; 11.
DR DIP; DIP-10412N; -.
DR STRING; 511145.b4162; -.
DR jPOST; P0A784; -.
DR PaxDb; P0A784; -.
DR PRIDE; P0A784; -.
DR EnsemblBacteria; AAC77122; AAC77122; b4162.
DR EnsemblBacteria; BAE78166; BAE78166; BAE78166.
DR GeneID; 67414780; -.
DR GeneID; 948675; -.
DR KEGG; ecj:JW5740; -.
DR KEGG; eco:b4162; -.
DR PATRIC; fig|1411691.4.peg.2536; -.
DR EchoBASE; EB2373; -.
DR eggNOG; COG1949; Bacteria.
DR HOGENOM; CLU_064761_2_0_6; -.
DR InParanoid; P0A784; -.
DR OMA; AFFHYRN; -.
DR PhylomeDB; P0A784; -.
DR BioCyc; EcoCyc:G7842-MON; -.
DR BioCyc; MetaCyc:G7842-MON; -.
DR BRENDA; 3.1.13.3; 2026.
DR EvolutionaryTrace; P0A784; -.
DR PRO; PR:P0A784; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0034611; F:oligoribonucleotidase activity; IDA:EcoCyc.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0006401; P:RNA catabolic process; IMP:EcoCyc.
DR CDD; cd06135; Orn; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00045; Oligoribonuclease; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR022894; Oligoribonuclease.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR11046; PTHR11046; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase;
KW Metal-binding; Nuclease; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9573169"
FT CHAIN 2..181
FT /note="Oligoribonuclease"
FT /id="PRO_0000111033"
FT DOMAIN 8..171
FT /note="Exonuclease"
FT ACT_SITE 129
FT /evidence="ECO:0000255"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2IGI"
FT STRAND 8..18
FT /evidence="ECO:0007829|PDB:2IGI"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2IGI"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:2IGI"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:2IGI"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:2IGI"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:2IGI"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:2IGI"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:2IGI"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2IGI"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2IGI"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:2IGI"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:2IGI"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2IGI"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:2IGI"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:2IGI"
FT HELIX 160..177
FT /evidence="ECO:0007829|PDB:2IGI"
SQ SEQUENCE 181 AA; 20816 MW; 57A5C7D500C4502F CRC64;
MSANENNLIW IDLEMTGLDP ERDRIIEIAT LVTDANLNIL AEGPTIAVHQ SDEQLALMDD
WNVRTHTASG LVERVKASTM GDREAELATL EFLKQWVPAG KSPICGNSIG QDRRFLFKYM
PELEAYFHYR YLDVSTLKEL ARRWKPEILD GFTKQGTHQA MDDIRESVAE LAYYREHFIK
L
