ID   RNH2_LACLA              Reviewed;         258 AA.
AC   Q9CG17;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Ribonuclease HII;
DE            Short=RNase HII;
DE            EC=3.1.26.4;
GN   Name=rnhB; OrderedLocusNames=LL1293; ORFNames=L0320;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK05391.1; -; Genomic_DNA.
DR   PIR; E86786; E86786.
DR   RefSeq; NP_267449.1; NC_002662.1.
DR   RefSeq; WP_003130174.1; NC_002662.1.
DR   AlphaFoldDB; Q9CG17; -.
DR   SMR; Q9CG17; -.
DR   STRING; 272623.L0320; -.
DR   PaxDb; Q9CG17; -.
DR   EnsemblBacteria; AAK05391; AAK05391; L0320.
DR   KEGG; lla:L0320; -.
DR   PATRIC; fig|272623.7.peg.1396; -.
DR   eggNOG; COG0164; Bacteria.
DR   HOGENOM; CLU_036532_2_1_9; -.
DR   OMA; YPTKLHL; -.
DR   Proteomes; UP000002196; 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;
KW   Reference proteome.
FT   CHAIN           1..258
FT                   /note="Ribonuclease HII"
FT                   /id="PRO_0000111583"
FT   DOMAIN          71..258
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   258 AA;  28525 MW;  F1CF958990E5C8FA CRC64;
     MGQTIKEIKA TLAKLTDLSA KEFLEYEADE RAGVQAALKS RKKQILAELA EEARLEQMLE
     FEKELYGQEI QLIAGIDEVG RGPLAGPVVT AAVILPKNCK IRGLNDSKKV PKSKHHAILS
     EIQEKALAIG IGIVDAEKID EVNIYEATKI AMIQAVSKLS VKPEHLLIDA MVLDFPIAQT
     KIIHGDARSA SIAAASIVAK VTRDEMMKEF ALEFPEYDFE HNAGYGTAKH LEALTKYGIT
     RIHRKSYEPI KTMVNFKS