ID   A0A269WBA8_9BACL        Unreviewed;       245 AA.
AC   A0A269WBA8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 9.
DE   SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:PAK55446.1};
GN   ORFNames=CHH75_04180 {ECO:0000313|EMBL:PAK55446.1};
OS   Paenibacillus sp. 7541.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2026236 {ECO:0000313|EMBL:PAK55446.1, ECO:0000313|Proteomes:UP000215741};
RN   [1] {ECO:0000313|EMBL:PAK55446.1, ECO:0000313|Proteomes:UP000215741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7541 {ECO:0000313|EMBL:PAK55446.1,
RC   ECO:0000313|Proteomes:UP000215741};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (AUG-2017) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAK55446.1}.
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DR   EMBL; NQLZ01000005; PAK55446.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A269WBA8; -.
DR   Proteomes; UP000215741; Unassembled WGS sequence.
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; PTHR42663:SF6; HYDROLASE C777.06C-RELATED; 1.
DR   PANTHER; PTHR42663; HYDROLASE C777.06C-RELATED-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:PAK55446.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215741}.
FT   DOMAIN          20..219
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   245 AA;  27905 MW;  537EF94E0512B282 CRC64;
     MSLKLQMLGT GSAFAKKYYN NNALLLDDDF TLLIDCGSTA PLALHEMGRS FNDIDAVLIT
     HIHADHVGGL EELAFMMKMK FKRRIPLYIG EALAAPLWDH TLRGGLYQQG EISCLEDIFD
     VRPLKPGVKA DISKGITVEL IQTRHIPGKD SYSLYLNDRI FYSADMVFDP ELLNKLVNER
     ECELILHECQ LQGPGEVHTT LQELLSLPEH IQQRTYLMHY SDDVQDFVGK TGEMEFVEQQ
     KIYEL
//