ID   A0A2V5K948_9BACL        Unreviewed;       286 AA.
AC   A0A2V5K948;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:PYI50310.1};
GN   ORFNames=DLM86_30025 {ECO:0000313|EMBL:PYI50310.1};
OS   Paenibacillus flagellatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2211139 {ECO:0000313|EMBL:PYI50310.1, ECO:0000313|Proteomes:UP000247476};
RN   [1] {ECO:0000313|EMBL:PYI50310.1, ECO:0000313|Proteomes:UP000247476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DXL2 {ECO:0000313|EMBL:PYI50310.1,
RC   ECO:0000313|Proteomes:UP000247476};
RA   Dai X.;
RT   "Paenibacillus flagellatus sp. nov., isolated from selenium mineral soil.";
RL   Submitted (MAY-2018) 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:PYI50310.1}.
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DR   EMBL; QJVJ01000020; PYI50310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5K948; -.
DR   OrthoDB; 9802248at2; -.
DR   Proteomes; UP000247476; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd07721; yflN-like_MBL-fold; 1.
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; PTHR42951:SF4; ACYL-COENZYME A THIOESTERASE MBLAC2; 1.
DR   PANTHER; PTHR42951; METALLO-BETA-LACTAMASE DOMAIN-CONTAINING; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:PYI50310.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247476}.
FT   DOMAIN          38..249
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   286 AA;  31312 MW;  32CC58313669005F CRC64;
     MEHNMTYGSD YSFIPAVSIG SGTGREVRPD IWCQTVQIVN VLFVGDPGRP DDWVLVDAGM
     PRSADAIVAA VRERFGSDRR PAAIVLTHGH FDHVGAIIEL VRHWEVPVYA HERELPYLTG
     KLDYPEPDSS VEGGLIAKMS PLFPNESIDL GDRVTALPAD GSVPGLPEWR WVHTPGHTPG
     HVSLFRERDR TLLAGDAFVT VRQDSLYSVL VQEQEISGPP RYLTPDWAAA RESVVRLAAL
     KPSVAATGHG VPMAGEPLAE GLSRLAAEFD RIAVPDYGRY VNDVNH
//