ID   RNH2_LACLM              Reviewed;         257 AA.
AC   O30415; A2RKF9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Ribonuclease HII;
DE            Short=RNase HII;
DE            EC=3.1.26.4;
GN   Name=rnhB; OrderedLocusNames=llmg_1176;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 92-257.
RX   PubMed=9484886; DOI=10.1046/j.1365-2958.1998.00676.x;
RA   Sanders J.W., Leenhouts K., Burghoorn J., Brands J.R., Venema G., Kok J.;
RT   "A chloride-inducible acid resistance mechanism in Lactococcus lactis and
RT   its regulation.";
RL   Mol. Microbiol. 27:299-310(1998).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000250}.
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; AM406671; CAL97769.1; -; Genomic_DNA.
DR   EMBL; AF005098; AAC46185.1; -; Genomic_DNA.
DR   RefSeq; WP_011835077.1; NC_009004.1.
DR   AlphaFoldDB; O30415; -.
DR   SMR; O30415; -.
DR   STRING; 416870.llmg_1176; -.
DR   EnsemblBacteria; CAL97769; CAL97769; llmg_1176.
DR   KEGG; llm:llmg_1176; -.
DR   eggNOG; COG0164; Bacteria.
DR   HOGENOM; CLU_036532_2_1_9; -.
DR   OMA; YPTKLHL; -.
DR   PhylomeDB; O30415; -.
DR   BioCyc; LLAC416870:LLMG_RS05955-MON; -.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Manganese; Metal-binding; Nuclease.
FT   CHAIN           1..257
FT                   /note="Ribonuclease HII"
FT                   /id="PRO_0000111584"
FT   DOMAIN          71..257
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         77
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   257 AA;  28439 MW;  E1767522FF30C943 CRC64;
     MGQTIKEIKA RLADLTDLSA KEFLEFETDE RAGVQAALKS RKKQILAECA EDERLEQMLE
     FEKELYSQEI ELIAGIDEVG RGPLAGPVVT AAVILPKNCK IRGLNDSKKV PKSKHHAILS
     EIQEKALAIG VGIVDAEKID EVNIYEATKI AMIQAVSKLS LKPEHLLIDA MVLDLPIAQT
     KIIHGDARSA SIAAASIVAK VTRDEMMKDF ALEFPEYDFE HNAGYGTAKH LAALTKYGIT
     RIHRKSYEPI KSMVNFK