ID L0EB57_THECK Unreviewed; 271 AA.
AC L0EB57;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Metal-dependent hydrolase, beta-lactamase superfamily I {ECO:0000313|EMBL:AGA56385.1};
GN OrderedLocusNames=Theco_0138 {ECO:0000313|EMBL:AGA56385.1};
OS Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA56385.1, ECO:0000313|Proteomes:UP000010795};
RN [1] {ECO:0000313|Proteomes:UP000010795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18247 / JCM 13945 / KWC4
RC {ECO:0000313|Proteomes:UP000010795};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA Woyke T.;
RT "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Counteracts the endogenous Pycsar antiviral defense system.
CC Phosphodiesterase that enables metal-dependent hydrolysis of host
CC cyclic nucleotide Pycsar defense signals such as cCMP and cUMP.
CC {ECO:0000256|ARBA:ARBA00034301}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic CMP + H2O = CMP + H(+); Xref=Rhea:RHEA:72675,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58003,
CC ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00034221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72676;
CC Evidence={ECO:0000256|ARBA:ARBA00034221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic UMP + H2O = H(+) + UMP; Xref=Rhea:RHEA:70575,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:184387; Evidence={ECO:0000256|ARBA:ARBA00034227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70576;
CC Evidence={ECO:0000256|ARBA:ARBA00034227};
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DR EMBL; CP003255; AGA56385.1; -; Genomic_DNA.
DR RefSeq; WP_015253152.1; NC_019897.1.
DR AlphaFoldDB; L0EB57; -.
DR STRING; 717605.Theco_0138; -.
DR KEGG; tco:Theco_0138; -.
DR eggNOG; COG1235; Bacteria.
DR HOGENOM; CLU_073253_0_0_9; -.
DR OrthoDB; 9781189at2; -.
DR Proteomes; UP000010795; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR47619; METALLO-HYDROLASE YYCJ-RELATED; 1.
DR PANTHER; PTHR47619:SF1; METALLO-HYDROLASE YYCJ-RELATED; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AGA56385.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010795}.
FT DOMAIN 13..218
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 271 AA; 30057 MW; A6B27E513F2AE6D8 CRC64;
MGLRFTILAS GSTGNATIVQ TDDVTLLIDA GLSAKKLEER MRERGIDASD IDAAFVTHEH
ADHVKGLGAF ARKYELPVYA NEATWSAMER QTAGIADANR KIVATGGEIE FGGLVVRSYP
ISHDAAEPVG YCFHEGGYKL SLVTDLGYFS DKVKEAVIDS DVVVLEANHD VEMLRMGRYP
WNIKRRILSD VGHLSNEAAG EALAELMTDR TKRVYLAHLS LDHNMQDLAR MTVESILESR
GIFLKKDDDV LKPTWHDRAT PWDDVTRRVI G
//
