ID A0A3Q8SAL8_9BACL Unreviewed; 305 AA.
AC A0A3Q8SAL8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:AZK46306.1};
GN ORFNames=EIM92_09055 {ECO:0000313|EMBL:AZK46306.1};
OS Paenibacillus lentus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1338368 {ECO:0000313|EMBL:AZK46306.1, ECO:0000313|Proteomes:UP000273145};
RN [1] {ECO:0000313|EMBL:AZK46306.1, ECO:0000313|Proteomes:UP000273145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25539 {ECO:0000313|EMBL:AZK46306.1,
RC ECO:0000313|Proteomes:UP000273145};
RA Kook J.-K., Park S.-N., Lim Y.K.;
RT "Genome sequencing of Paenibacillus lentus DSM25539(T).";
RL Submitted (NOV-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP034248; AZK46306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q8SAL8; -.
DR KEGG; plen:EIM92_09055; -.
DR OrthoDB; 9761531at2; -.
DR Proteomes; UP000273145; Chromosome.
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; PTHR30619; DNA INTERNALIZATION/COMPETENCE PROTEIN COMEC/REC2; 1.
DR PANTHER; PTHR30619:SF1; RECOMBINATION PROTEIN 2; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AZK46306.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000273145}.
FT DOMAIN 21..95
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF00753"
FT COILED 149..176
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 305 AA; 34403 MW; D90FC47397B8A307 CRC64;
MTYVIDFLNV GFGEAAVVRI EDGQRSYCLV VDAGDADCHK HARRCSLEQY VREYGINKID
ALILTHFHKD HIGGVREVLG HVPIGEILLH VPLPSHLLNS RLSDHSTPIL ASLSLYIAIL
KQAKELGIPV RQISEPFALS ELAVEFRLLT PNQAKLQQLQ AELESLEVEA LNRQQERLTR
IDRMLNDTAL AVLIRYKHNP AALLTSDVGL DFWSPYESEI KDVYLLQAPH HGDAQRISQA
LLHTVSPKVV VVSADDEGTY QLPHPEFEVA VTEHSAARIY YTEEAGSRHR IIRMDLNERT
IHLIK
//