ID G4HLQ7_9BACL Unreviewed; 227 AA.
AC G4HLQ7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=UPF0173 metal-dependent hydrolase PaelaDRAFT_4918 {ECO:0000256|HAMAP-Rule:MF_00457};
GN ORFNames=PaelaDRAFT_4918 {ECO:0000313|EMBL:EHB56983.1};
OS Paenibacillus lactis 154.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB56983.1, ECO:0000313|Proteomes:UP000003891};
RN [1] {ECO:0000313|EMBL:EHB56983.1, ECO:0000313|Proteomes:UP000003891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=154 {ECO:0000313|EMBL:EHB56983.1,
RC ECO:0000313|Proteomes:UP000003891};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA Allgaier M., Woyke T.J.;
RT "The draft genome of Paenibacillus lactis 154.";
RL Submitted (SEP-2011) 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; AGIP01000014; EHB56983.1; -; Genomic_DNA.
DR RefSeq; WP_007132078.1; NZ_AGIP01000014.1.
DR AlphaFoldDB; G4HLQ7; -.
DR STRING; 743719.PaelaDRAFT_4918; -.
DR PATRIC; fig|743719.3.peg.5002; -.
DR eggNOG; COG2220; Bacteria.
DR OrthoDB; 9789133at2; -.
DR Proteomes; UP000003891; 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; PF13483; Lactamase_B_3; 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}.
FT DOMAIN 7..191
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 227 AA; 24100 MW; 3F71C6B09440066A CRC64;
MKITYYGHSS ILVEAGGKSV IIDPFLSGNP GSGISPSDVK VDAVVLTHGH SDHFGDCIEI
AKNNDCPVIA VYELAVYCGN QGVKSHGMNI GGSAKFDGFK VKYTPAFHSS SISVGDTWIY
AGQPGGVILT MGDKQFYHAG DTSLFGDMKL IGEMNNIDAA ALPIGDMLTM GPEDALLAAQ
WIRTKHVIPV HYDTFPGIRQ DAQAFCEELA KTGVSGHPLK AGESLEI
//
