ID   A0A1H4K0G2_9BACL        Unreviewed;       232 AA.
AC   A0A1H4K0G2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=UPF0173 metal-dependent hydrolase SAMN05443246_0852 {ECO:0000256|HAMAP-Rule:MF_00457};
GN   ORFNames=SAMN05443246_0852 {ECO:0000313|EMBL:SEB52021.1};
OS   Paenibacillus sp. GP183.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1882751 {ECO:0000313|EMBL:SEB52021.1, ECO:0000313|Proteomes:UP000199177};
RN   [1] {ECO:0000313|EMBL:SEB52021.1, ECO:0000313|Proteomes:UP000199177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP183 {ECO:0000313|EMBL:SEB52021.1,
RC   ECO:0000313|Proteomes:UP000199177};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
CC   -!- SIMILARITY: Belongs to the UPF0173 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00457}.
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DR   EMBL; FNSW01000001; SEB52021.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4K0G2; -.
DR   STRING; 1882751.SAMN05443246_0852; -.
DR   OrthoDB; 9789133at2; -.
DR   Proteomes; UP000199177; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   HAMAP; MF_00457; UPF0173; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR022877; UPF0173.
DR   PANTHER; PTHR43546:SF3; UPF0173 METAL-DEPENDENT HYDROLASE MJ1163; 1.
DR   PANTHER; PTHR43546; UPF0173 METAL-DEPENDENT HYDROLASE MJ1163-RELATED; 1.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00457};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199177}.
FT   DOMAIN          7..193
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   232 AA;  24995 MW;  899F6D2593608D1C CRC64;
     MIITFLGHSC VQLQTEHHTL IIDPFITGNP AAKVSASDLK VDAVLLTHGH GDHVGDAADI
     AKRNDALLVA PNELAVYMGW QGCKVHPMHI GGAHTFEFGK VKLTQAFHGS GYEIPDKKVI
     VYMGMPAGML LYVDGLTIYH SGDTSLFGDM KIIGELNDID LAFLPIGDNF TMGPEDAVLA
     AKWLGAKKVV PVHYNTFPLI AQDGHAFAKA LAEHQIEGIV MESGDSLKLD GR
//