RNH2_ECOLI
ID RNH2_ECOLI Reviewed; 198 AA.
AC P10442; P78265;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ribonuclease HII;
DE Short=RNase HII;
DE EC=3.1.26.4;
GN Name=rnhB; OrderedLocusNames=b0183, JW0178;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3316192; DOI=10.1128/jb.169.12.5735-5744.1987;
RA Tomasiewicz H.G., McHenry C.S.;
RT "Sequence analysis of the Escherichia coli dnaE gene.";
RL J. Bacteriol. 169:5735-5744(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
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], AND SEQUENCE REVISION TO
RP 196-198.
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 PROTEIN SEQUENCE OF 1-11, AND FUNCTION.
RC STRAIN=K12;
RX PubMed=2172991; DOI=10.1073/pnas.87.21.8587;
RA Itaya M.;
RT "Isolation and characterization of a second RNase H (RNase HII) of
RT Escherichia coli K-12 encoded by the rnhB gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8587-8591(1990).
RN [7]
RP CHARACTERIZATION.
RX PubMed=9888800; DOI=10.1021/bi982207z;
RA Ohtani N., Haruki M., Morikawa M., Crouch R.J., Itaya M., Kanaya S.;
RT "Identification of the genes encoding Mn2+-dependent RNase HII and Mg2+-
RT dependent RNase HIII from Bacillus subtilis: classification of RNases H
RT into three families.";
RL Biochemistry 38:605-618(1999).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000250, ECO:0000269|PubMed:2172991}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC the absence of substrate. May bind a second metal ion after substrate
CC binding. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000305}.
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DR EMBL; M19334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U70214; AAB08612.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73294.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77858.2; -; Genomic_DNA.
DR PIR; G64742; QQECBE.
DR RefSeq; NP_414725.1; NC_000913.3.
DR RefSeq; WP_000569430.1; NZ_SSZK01000004.1.
DR AlphaFoldDB; P10442; -.
DR SMR; P10442; -.
DR BioGRID; 4261585; 101.
DR IntAct; P10442; 5.
DR STRING; 511145.b0183; -.
DR jPOST; P10442; -.
DR PaxDb; P10442; -.
DR PRIDE; P10442; -.
DR EnsemblBacteria; AAC73294; AAC73294; b0183.
DR EnsemblBacteria; BAA77858; BAA77858; BAA77858.
DR GeneID; 66671529; -.
DR GeneID; 944852; -.
DR KEGG; ecj:JW0178; -.
DR KEGG; eco:b0183; -.
DR PATRIC; fig|1411691.4.peg.2096; -.
DR EchoBASE; EB0854; -.
DR eggNOG; COG0164; Bacteria.
DR HOGENOM; CLU_036532_3_2_6; -.
DR InParanoid; P10442; -.
DR OMA; YPTKLHL; -.
DR PhylomeDB; P10442; -.
DR BioCyc; EcoCyc:EG10861-MON; -.
DR BioCyc; MetaCyc:EG10861-MON; -.
DR BRENDA; 3.1.26.4; 2026.
DR PRO; PR:P10442; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:EcoCyc.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR CDD; cd07182; RNase_HII_bacteria_HII_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00052_B; RNase_HII_B; 1.
DR InterPro; IPR022898; RNase_HII.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR PANTHER; PTHR10954:SF18; PTHR10954:SF18; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Endonuclease; Hydrolase; Manganese;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..198
FT /note="Ribonuclease HII"
FT /id="PRO_0000111571"
FT DOMAIN 10..198
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 16
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT CONFLICT 196..198
FT /note="LAS -> TCVLILVSRLSKPESEDV (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21526 MW; 25350722EB5D7864 CRC64;
MIEFVYPHTQ LVAGVDEVGR GPLVGAVVTA AVILDPARPI AGLNDSKKLS EKRRLALYEE
IKEKALSWSL GRAEPHEIDE LNILHATMLA MQRAVAGLHI APEYVLIDGN RCPKLPMPAM
AVVKGDSRVP EISAASILAK VTRDAEMAAL DIVFPQYGFA QHKGYPTAFH LEKLAEHGAT
EHHRRSFGPV KRALGLAS
