RNHL_BACSU
ID RNHL_BACSU Reviewed; 132 AA.
AC P54162;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=14.7 kDa ribonuclease H-like protein;
GN Name=rnhA; Synonyms=ypdQ; OrderedLocusNames=BSU21990;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8969496; DOI=10.1099/13500872-142-11-3005;
RA Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT "Organization of the Bacillus subtilis 168 chromosome between kdg and the
RT attachment site of the SP beta prophage: use of long accurate PCR and yeast
RT artificial chromosomes for sequencing.";
RL Microbiology 142:3005-3015(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=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 [4]
RP MUTAGENESIS OF TRP-109.
RX PubMed=15115438; DOI=10.1042/bj20040153;
RA Ohtani N., Yanagawa H., Tomita M., Itaya M.;
RT "Identification of the first archaeal Type 1 RNase H gene from
RT Halobacterium sp. NRC-1: archaeal RNase HI can cleave an RNA-DNA
RT junction.";
RL Biochem. J. 381:795-802(2004).
CC -!- FUNCTION: Not known; does not have RNase H activity.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000305};
CC -!- SIMILARITY: Belongs to the RNase H family. EbsB subfamily.
CC {ECO:0000305}.
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DR EMBL; L77246; AAA96618.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14117.1; -; Genomic_DNA.
DR PIR; D69934; D69934.
DR RefSeq; NP_390082.1; NC_000964.3.
DR RefSeq; WP_003230765.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54162; -.
DR SMR; P54162; -.
DR STRING; 224308.BSU21990; -.
DR PaxDb; P54162; -.
DR PRIDE; P54162; -.
DR EnsemblBacteria; CAB14117; CAB14117; BSU_21990.
DR GeneID; 939074; -.
DR KEGG; bsu:BSU21990; -.
DR PATRIC; fig|224308.179.peg.2401; -.
DR eggNOG; COG0328; Bacteria.
DR InParanoid; P54162; -.
DR OMA; NTDHERW; -.
DR PhylomeDB; P54162; -.
DR BioCyc; BSUB:BSU21990-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF13456; RVT_3; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome.
FT CHAIN 1..132
FT /note="14.7 kDa ribonuclease H-like protein"
FT /id="PRO_0000195431"
FT DOMAIN 1..127
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 46
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 70
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 119
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT MUTAGEN 109
FT /note="W->H: Does not confer RNase H activity."
FT /evidence="ECO:0000269|PubMed:15115438"
SQ SEQUENCE 132 AA; 14670 MW; 3D52E492BB541E15 CRC64;
MPTEIYVDGA SAGNPGPSGI GIFIKHEGKA ESFSIPIGVH TNQEAEFLAL IEGMKLCATR
GYQSVSFRTD SDIVERATEL EMVKNITFQP FVEEIIRLKA AFPLFFIKWI PGKQNQKADL
LAKEAIRLNE KN
