ID A0A0U2N713_9BACL Unreviewed; 258 AA.
AC A0A0U2N713;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:ALS27967.1};
GN ORFNames=IJ21_25710 {ECO:0000313|EMBL:ALS27967.1};
OS Paenibacillus sp. 32O-W.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1695218 {ECO:0000313|EMBL:ALS27967.1, ECO:0000313|Proteomes:UP000059673};
RN [1] {ECO:0000313|Proteomes:UP000059673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-W {ECO:0000313|Proteomes:UP000059673};
RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT "Complete genome sequences of two moderately thermophilic Paenibacillus
RT species.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALS27967.1, ECO:0000313|Proteomes:UP000059673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-W {ECO:0000313|EMBL:ALS27967.1,
RC ECO:0000313|Proteomes:UP000059673};
RX PubMed=26868401;
RA Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL Genome Announc. 4:e01717-15(2016).
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; CP013653; ALS27967.1; -; Genomic_DNA.
DR RefSeq; WP_062492934.1; NZ_CP013653.1.
DR AlphaFoldDB; A0A0U2N713; -.
DR STRING; 1695218.IJ21_25710; -.
DR KEGG; pow:IJ21_25710; -.
DR PATRIC; fig|1695218.3.peg.2736; -.
DR OrthoDB; 9800940at2; -.
DR Proteomes; UP000059673; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd16279; metallo-hydrolase-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; 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:ALS27967.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059673}.
FT DOMAIN 37..230
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 258 AA; 29322 MW; 5B97BE46D07023E4 CRC64;
MTTITFRGTG DSMGVPRVYC DCAVCEEARA TGRNRRLRSL VQIDDPSLGT VLIDCGPDWR
RQMEAAGLRR VDVILLTHAH FDHIGGLAEW ADACRWTKER GLAYAPAEVI EEVLARFPWL
GRHIDFRPLS REETLGRWTV AAWKVNHGKN GYSYAYRFDR PNGGPAWVYC PDAIGLTEEM
LRPMRGLDLL VLGTSFYHEP YPYETRSVYD VTEALELAAE LRPRRMVLTH QSHDIDLRRD
YGLPAHVAFA ETGMTVTL
//
