RNH3_BACSU
ID RNH3_BACSU Reviewed; 313 AA.
AC P94541;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ribonuclease HIII;
DE Short=RNase HIII;
DE EC=3.1.26.4;
GN Name=rnhC; Synonyms=ysgB; OrderedLocusNames=BSU28620;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10094689; DOI=10.1128/jb.181.7.2118-2123.1999;
RA Itaya M., Omori A., Kanaya S., Crouch R.J., Tanaka T., Kondo K.;
RT "Isolation of RNase H genes that are essential for growth of Bacillus
RT subtilis 168.";
RL J. Bacteriol. 181:2118-2123(1999).
RN [4]
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).
RN [5]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=21710567; DOI=10.1002/pmic.201000790;
RA Delumeau O., Lecointe F., Muntel J., Guillot A., Guedon E., Monnet V.,
RA Hecker M., Becher D., Polard P., Noirot P.;
RT "The dynamic protein partnership of RNA polymerase in Bacillus subtilis.";
RL Proteomics 11:2992-3001(2011).
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 -!- SUBUNIT: Interacts with the RNA polymerase core.
CC {ECO:0000269|PubMed:21710567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC {ECO:0000305}.
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DR EMBL; Z75208; CAA99565.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14822.1; -; Genomic_DNA.
DR PIR; H69984; H69984.
DR RefSeq; NP_390740.1; NC_000964.3.
DR RefSeq; WP_003245949.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P94541; -.
DR SMR; P94541; -.
DR STRING; 224308.BSU28620; -.
DR PaxDb; P94541; -.
DR PRIDE; P94541; -.
DR EnsemblBacteria; CAB14822; CAB14822; BSU_28620.
DR GeneID; 937436; -.
DR KEGG; bsu:BSU28620; -.
DR PATRIC; fig|224308.179.peg.3109; -.
DR eggNOG; COG1039; Bacteria.
DR InParanoid; P94541; -.
DR OMA; TGDYFGP; -.
DR PhylomeDB; P94541; -.
DR BioCyc; BSUB:BSU28620-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IBA:GO_Central.
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; cd14796; RNAse_HIII_N; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00053; RNase_HIII; 1.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR004641; RNase_HIII.
DR InterPro; IPR024568; RNase_HIII_N.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR Pfam; PF11858; DUF3378; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR PIRSF; PIRSF037748; RnhC; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00716; rnhC; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..313
FT /note="Ribonuclease HIII"
FT /id="PRO_0000111680"
FT DOMAIN 94..310
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT REGION 63..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 313 AA; 34070 MW; 827E691FA6DA30A4 CRC64;
MSHSVIKVSL SAIDQMKMTY SGSLTASVPQ GAVFQAKPPG CTITAYQSGK VLFQGKNAAA
ESARWGTAEP QEKKKTAKKP ADPRYAPPAD IAGMSVIGSD EVGTGDYFGP MTVVCAYVDK
TMLPLMKELG VKDSKDLKDP QIIEIARNLI KTIPYSLLVL KNEKYNSMQE KGMSQGKMKA
LLHNQAITHL LRKLDGVKPE AILIDQFAEP GVYFNHLKGR DIVKERTYFS TKAEGIHLAV
AAASIIARYS FLMEMDKLSR AAGMTLPKGA GPHVDEAAAK LILKKGASAL RTFTKLHFAN
TQKAQRLADK KRS
