ID C6J5Y0_9BACL Unreviewed; 286 AA.
AC C6J5Y0;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Metallo-beta-lactamase domain-containing protein {ECO:0000259|Pfam:PF12706};
GN ORFNames=POTG_03784 {ECO:0000313|EMBL:EES71561.1};
OS Paenibacillus sp. oral taxon 786 str. D14.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=621372 {ECO:0000313|EMBL:EES71561.1, ECO:0000313|Proteomes:UP000003981};
RN [1] {ECO:0000313|EMBL:EES71561.1, ECO:0000313|Proteomes:UP000003981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D14 {ECO:0000313|EMBL:EES71561.1,
RC ECO:0000313|Proteomes:UP000003981};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., White A.,
RA Lander E., Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Paenibacillus sp. D14.";
RL Submitted (MAR-2009) 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};
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DR EMBL; GG695991; EES71561.1; -; Genomic_DNA.
DR RefSeq; WP_009226502.1; NZ_GG695991.1.
DR AlphaFoldDB; C6J5Y0; -.
DR eggNOG; COG2220; Bacteria.
DR HOGENOM; CLU_020884_3_0_9; -.
DR OrthoDB; 9800061at2; -.
DR Proteomes; UP000003981; Unassembled WGS sequence.
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; 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 SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000003981}.
FT DOMAIN 44..240
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
SQ SEQUENCE 286 AA; 32309 MW; A6EE606CCBF64DCD CRC64;
MTQNQRTGAA LIREIARTKA PYGTLAIWYL GQESVIVKGD GITIYVDPYL SGDLDDGDWR
RTFPAPIAPE EIEGVQLCLI THEHDDHMDA RTLPWLHRSS PEAPILAPAC CKPALQEMGL
PDSLLITADD RKPMEFFSKL RVTPIAAAHE QLERDADGCP RYVGYVLELN GVTLYHAGDT
LVFPELIKRV GELKPDIALL PINGRDYFRQ RRGIVGNMDY REAAHFAQEI GVDTVIPLHY
DLFAVNAEKP GHFVDYVYEH FPEQKVHVMA RAERFLYVSP RAFLLD
//
