ID A0A1K1NI18_9BACL Unreviewed; 233 AA.
AC A0A1K1NI18;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=UPF0173 metal-dependent hydrolase SAMN02799630_02317 {ECO:0000256|HAMAP-Rule:MF_00457};
GN ORFNames=SAMN02799630_02317 {ECO:0000313|EMBL:SFW34959.1};
OS Paenibacillus sp. UNCCL117.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1502764 {ECO:0000313|EMBL:SFW34959.1, ECO:0000313|Proteomes:UP000182480};
RN [1] {ECO:0000313|EMBL:SFW34959.1, ECO:0000313|Proteomes:UP000182480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCCL117 {ECO:0000313|EMBL:SFW34959.1,
RC ECO:0000313|Proteomes:UP000182480};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FPIU01000007; SFW34959.1; -; Genomic_DNA.
DR RefSeq; WP_072329662.1; NZ_FPIU01000007.1.
DR AlphaFoldDB; A0A1K1NI18; -.
DR STRING; 1502764.SAMN02799630_02317; -.
DR OrthoDB; 9789133at2; -.
DR Proteomes; UP000182480; 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; PF12706; Lactamase_B_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000182480}.
FT DOMAIN 7..194
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 233 AA; 25130 MW; 0A39C6EF06E88571 CRC64;
MQLTYHGHSC VQIASGGQSL IIDPFLRGNE LAVTAPEDIR TNAVLLTHAH ADHITDADLI
AKANDAPVVA TFELAAYMSW QGVRTIDMNM GGTVDLGFAK AKMIQAFHSS GIIVDDEKRI
VYGGMPGGYI VTAGGFTVLH AGDTCLFSDM KLIGERHAPI DVAFIPIGDR YTMGPDDALQ
AAEWYGARLT IPVHYDTFGV IRQDAEAFVR QLAERGMQGR VLRPGESLTI GAE
//
