RNI_ECOLI
ID RNI_ECOLI Reviewed; 268 AA.
AC P21338; P77101;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ribonuclease I;
DE Short=RNase I;
DE EC=4.6.1.21;
DE AltName: Full=Enterobacter ribonuclease;
DE Flags: Precursor;
GN Name=rna; Synonyms=rnsA; OrderedLocusNames=b0611, JW0603;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-63.
RC STRAIN=K12;
RX PubMed=2253883; DOI=10.1016/0378-1119(90)90406-h;
RA Meador J. III, Kennell D.;
RT "Cloning and sequencing the gene encoding Escherichia coli ribonuclease I:
RT exact physical mapping using the genome library.";
RL Gene 95:1-7(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP SIMILARITY TO FUNGAL RIBONUCLEASES.
RX PubMed=8188249; DOI=10.1006/geno.1994.1018;
RA Henikoff S., Henikoff J.G.;
RT "Protein family classification based on searching a database of blocks.";
RL Genomics 19:97-107(1994).
CC -!- FUNCTION: One of the few RNases that cleaves the phosphodiester bond
CC between any two nucleotide. Shows a preference for cytidylic or
CC guanylic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA containing adenosine-cytidine + H2O = an [RNA fragment]-
CC 3'-cytidine-3'-phosphate + a 5'-a hydroxy-adenosine -3'-[RNA
CC fragment].; EC=4.6.1.21;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Periplasm. Cytoplasm. Note=RNase I (periplasmic)
CC and RNase I* (cytoplasmic) appear to be isoforms apparently encoded by
CC the same gene. The cytoplasmic form is less active towards natural
CC polymer RNA.
CC -!- PTM: Contains four disulfide bonds. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40811.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M55687; AAA24548.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40811.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73712.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35240.1; -; Genomic_DNA.
DR PIR; JQ0777; JQ0777.
DR RefSeq; NP_415144.1; NC_000913.3.
DR RefSeq; WP_000643397.1; NZ_SSZK01000032.1.
DR PDB; 2EA1; X-ray; 1.80 A; A=24-268.
DR PDB; 2PQX; X-ray; 1.42 A; A=24-268.
DR PDB; 2PQY; X-ray; 2.30 A; A=24-268.
DR PDB; 2Z70; X-ray; 1.70 A; A=24-268.
DR PDBsum; 2EA1; -.
DR PDBsum; 2PQX; -.
DR PDBsum; 2PQY; -.
DR PDBsum; 2Z70; -.
DR AlphaFoldDB; P21338; -.
DR SMR; P21338; -.
DR BioGRID; 4259901; 35.
DR IntAct; P21338; 1.
DR STRING; 511145.b0611; -.
DR jPOST; P21338; -.
DR PaxDb; P21338; -.
DR PRIDE; P21338; -.
DR EnsemblBacteria; AAC73712; AAC73712; b0611.
DR EnsemblBacteria; BAA35240; BAA35240; BAA35240.
DR GeneID; 58462622; -.
DR GeneID; 949065; -.
DR KEGG; ecj:JW0603; -.
DR KEGG; eco:b0611; -.
DR PATRIC; fig|1411691.4.peg.1657; -.
DR EchoBASE; EB0849; -.
DR eggNOG; COG3719; Bacteria.
DR HOGENOM; CLU_066430_1_0_6; -.
DR InParanoid; P21338; -.
DR OMA; RVRMRCQ; -.
DR PhylomeDB; P21338; -.
DR BioCyc; EcoCyc:EG10856-MON; -.
DR BioCyc; MetaCyc:EG10856-MON; -.
DR BRENDA; 4.6.1.18; 2026.
DR EvolutionaryTrace; P21338; -.
DR PRO; PR:P21338; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0008847; F:Enterobacter ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IMP:EcoCyc.
DR CDD; cd01062; RNase_T2_prok; 1.
DR Gene3D; 3.90.730.10; -; 1.
DR InterPro; IPR001568; RNase_T2-like.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR018188; RNase_T2_His_AS_1.
DR InterPro; IPR033130; RNase_T2_His_AS_2.
DR InterPro; IPR039378; RNase_T2_prok.
DR PANTHER; PTHR11240; PTHR11240; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR PROSITE; PS00530; RNASE_T2_1; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Endonuclease; Hydrolase; Lyase; Nuclease; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2253883"
FT CHAIN 24..268
FT /note="Ribonuclease I"
FT /id="PRO_0000030961"
FT ACT_SITE 78
FT /evidence="ECO:0000250"
FT ACT_SITE 152
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /evidence="ECO:0000250"
FT DISULFID 103..159
FT /evidence="ECO:0000250"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2PQX"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:2PQX"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2PQX"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2PQX"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:2PQX"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 164..180
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2PQX"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2PQX"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:2PQX"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2PQX"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:2PQX"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:2PQX"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:2PQX"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2PQY"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:2PQX"
SQ SEQUENCE 268 AA; 29618 MW; 56BC290438EE3DD0 CRC64;
MKAFWRNAAL LAVSLLPFSS ANALALQAKQ YGDFDRYVLA LSWQTGFCQS QHDRNRNERD
ECRLQTETTN KADFLTVHGL WPGLPKSVAA RGVDERRWMR FGCATRPIPN LPEARASRMC
SSPETGLSLE TAAKLSEVMP GAGGRSCLER YEYAKHGACF GFDPDAYFGT MVRLNQEIKE
SEAGKFLADN YGKTVSRRDF DAAFAKSWGK ENVKAVKLTC QGNPAYLTEI QISIKADAIN
APLSANSFLP QPHPGNCGKT FVIDKAGY
