ID A0A089LQ42_9BACL Unreviewed; 249 AA.
AC A0A089LQ42;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:AIQ63666.1};
GN ORFNames=PSTEL_11825 {ECO:0000313|EMBL:AIQ63666.1};
OS Paenibacillus stellifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ63666.1, ECO:0000313|Proteomes:UP000029507};
RN [1] {ECO:0000313|EMBL:AIQ63666.1, ECO:0000313|Proteomes:UP000029507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ63666.1,
RC ECO:0000313|Proteomes:UP000029507};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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; CP009286; AIQ63666.1; -; Genomic_DNA.
DR RefSeq; WP_038695371.1; NZ_CP009286.1.
DR AlphaFoldDB; A0A089LQ42; -.
DR STRING; 169760.PSTEL_11825; -.
DR KEGG; pste:PSTEL_11825; -.
DR HOGENOM; CLU_030571_2_1_9; -.
DR OrthoDB; 9802248at2; -.
DR Proteomes; UP000029507; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd07721; yflN-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; PTHR42951; METALLO-BETA-LACTAMASE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR42951:SF15; METALLO-BETA-LACTAMASE SUPERFAMILY PROTEIN; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AIQ63666.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029507}.
FT DOMAIN 22..230
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 249 AA; 26987 MW; 755EE3800A2E1832 CRC64;
MRIAEGLEML EIEAQIMGGS ERIYPVLMWD DEHVMLVDTG YPGITETFQA GFAEAGVAWD
RLDTVLITHQ DLDHIGGLPA ILEQRPSIRV LAHPLERPYI EGERMLLKHT PEAIAAAEAM
LPPNVPAEWR RAFLHVLSHP PRARVDAELT DGEVLQVAGG VTVITTPGHS PGHVSLYHDA
SGTLVAGDSL TVKDGELHGP DPRATPDMPA ALASLRRYAG LTIHTVICYH GGLYRGDAGK
RIAELAEGK
//
