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RBN_KLEP7
ID   RBN_KLEP7               Reviewed;         306 AA.
AC   A6TBW1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Ribonuclease BN {ECO:0000255|HAMAP-Rule:MF_01818};
DE            Short=RNase BN {ECO:0000255|HAMAP-Rule:MF_01818};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01818};
DE   AltName: Full=Ribonuclease Z homolog {ECO:0000255|HAMAP-Rule:MF_01818};
DE            Short=RNase Z homolog {ECO:0000255|HAMAP-Rule:MF_01818};
GN   Name=rbn {ECO:0000255|HAMAP-Rule:MF_01818}; Synonyms=rnz;
GN   OrderedLocusNames=KPN78578_26210; ORFNames=KPN_02665;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Zinc phosphodiesterase, which has both exoribonuclease and
CC       endoribonuclease activities. {ECO:0000255|HAMAP-Rule:MF_01818}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01818};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_01818};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01818}.
CC   -!- SIMILARITY: Belongs to the RNase Z family. RNase BN subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01818}.
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DR   EMBL; CP000647; ABR78082.1; -; Genomic_DNA.
DR   RefSeq; WP_015958759.1; NC_009648.1.
DR   AlphaFoldDB; A6TBW1; -.
DR   SMR; A6TBW1; -.
DR   STRING; 272620.KPN_02665; -.
DR   EnsemblBacteria; ABR78082; ABR78082; KPN_02665.
DR   KEGG; kpn:KPN_02665; -.
DR   HOGENOM; CLU_031317_2_0_6; -.
DR   OMA; GTQRQMM; -.
DR   Proteomes; UP000000265; Chromosome.
DR   GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042779; P:tRNA 3'-trailer cleavage; IEA:InterPro.
DR   CDD; cd07717; RNaseZ_ZiPD-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_01818; RNase_Z_BN; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR013471; RNase_Z/BN.
DR   Pfam; PF12706; Lactamase_B_2; 2.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR02651; RNase_Z; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..306
FT                   /note="Ribonuclease BN"
FT                   /id="PRO_1000070283"
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
SQ   SEQUENCE   306 AA;  33487 MW;  93407D058631859E CRC64;
     MELTFLGTSA GVPTRTRNMT SIILNLQQPT RAEMWLFDCG EGTQHQFLHT PYHPGKLNKI
     FITHLHGDHL FGLPGLLCSR SMQGNSLPLT LYGPKGLKEF VETALRLSGS WTDYPLTIIE
     VGPGLVFDEE GYRVTAYPLS HPVECYGYRI AQHDKPGTLD AAQLIADGVP PGPLFHQLKR
     GQRVELADGR VIDGSRYLGP STPGKTLAIF GDTAPCPQAL EMARGADVMV HETTLEQAMA
     EKANSRGHSS SQQTAALAKE AGVGTLIATH FSSRYDAEGC LRMLAECREI FPNTLLAEDF
     MVYKMA
 
 
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