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Database: UniProt
Entry: H6R9T3_NOCCG
LinkDB: H6R9T3_NOCCG
Original site: H6R9T3_NOCCG 
ID   H6R9T3_NOCCG            Unreviewed;       263 AA.
AC   H6R9T3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative hydrolase {ECO:0000313|EMBL:CCF61141.1};
GN   OrderedLocusNames=NOCYR_0321 {ECO:0000313|EMBL:CCF61141.1};
OS   Nocardia cyriacigeorgica (strain GUH-2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF61141.1, ECO:0000313|Proteomes:UP000008190};
RN   [1] {ECO:0000313|EMBL:CCF61141.1, ECO:0000313|Proteomes:UP000008190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GUH-2 {ECO:0000313|EMBL:CCF61141.1,
RC   ECO:0000313|Proteomes:UP000008190};
RX   PubMed=22461543; DOI=10.1128/JB.00161-12;
RA   Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA   Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA   Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA   Richard Y., Cournoyer B., Blaha D.;
RT   "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT   cyriacigeorgica GUH-2.";
RL   J. Bacteriol. 194:2098-2099(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; FO082843; CCF61141.1; -; Genomic_DNA.
DR   RefSeq; WP_014348618.1; NC_016887.1.
DR   AlphaFoldDB; H6R9T3; -.
DR   STRING; 1127134.NOCYR_0321; -.
DR   KEGG; ncy:NOCYR_0321; -.
DR   eggNOG; COG0491; Bacteria.
DR   HOGENOM; CLU_048478_2_0_11; -.
DR   OrthoDB; 9788263at2; -.
DR   Proteomes; UP000008190; Chromosome.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR   CDD; cd16278; metallo-hydrolase-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR001018; Beta-lactamase_class-B_CS.
DR   InterPro; IPR041516; LACTB2_WH.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR23131; ENDORIBONUCLEASE LACTB2; 1.
DR   PANTHER; PTHR23131:SF0; ENDORIBONUCLEASE LACTB2; 1.
DR   Pfam; PF17778; BLACT_WH; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS00743; BETA_LACTAMASE_B_1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCF61141.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008190}.
FT   DOMAIN          33..191
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   263 AA;  28046 MW;  DF012969F451D761 CRC64;
     MTLTHPAYGQ LRQVTPTAAV LLADNPGQMT LDGTNTWILR APDGAGYVVV DPGPKQRAHI
     EAIAAATGGD IALTLITHRH SDHTGGIDRL VKLTGTPVRA MDREFLRGSD AVLTDGEVIV
     AGGLRITVLH TPGHTGDSVS FVLDDAVLTG DTILGRGTTV LESAEGALGN YLRSLDRLVE
     VGAGKALLPA HGPDHPDLEP VARYYIEHRQ ERLEQVRAAL AELGPDAGPM AVVRKVYADV
     DKKLWLAARS SVQAQLEYLR SQP
//
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