ID A0A433X4K4_9BACL Unreviewed; 324 AA.
AC A0A433X4K4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:RUT28951.1};
GN ORFNames=EJP77_16220 {ECO:0000313|EMBL:RUT28951.1};
OS Paenibacillus zeisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2496267 {ECO:0000313|EMBL:RUT28951.1, ECO:0000313|Proteomes:UP000272464};
RN [1] {ECO:0000313|EMBL:RUT28951.1, ECO:0000313|Proteomes:UP000272464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-5-3 {ECO:0000313|EMBL:RUT28951.1,
RC ECO:0000313|Proteomes:UP000272464};
RA Sun L., Chen Z.;
RL Submitted (DEC-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUT28951.1}.
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; RZNX01000008; RUT28951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433X4K4; -.
DR OrthoDB; 9805728at2; -.
DR Proteomes; UP000272464; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR024884; NAPE-PLD.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR15032:SF36; LACTAMASE_B DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR15032; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR PIRSF; PIRSF038896; NAPE-PLD; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:RUT28951.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000272464}.
FT DOMAIN 74..271
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
SQ SEQUENCE 324 AA; 37957 MW; 77A92DC6EB8D78FD CRC64;
MPRHRFNNID NVSTDKTLKQ FSQWREERRR KKKDYSYVIP NSEPELEYLR NNREDTTITW
IGHSTFLIQY HGLNIVTDPV WAPRMAFQRR LGSPGIPIDE IPEVDIILIS HSHYDHMHIS
SIRKLYGART TILVPVGLKR KMERKGFSRC EEMKWWEELT VKNVKFSFVP TQHWTRRTPF
DTNTSHWGGF VMEIDPPEQK GQGDPVIYFA GDSGYFKGFK DIGERYNIDV ALMPIGAYEP
EWFMTSQHVN PEEAIQAFVD VKAKTMVPMH YGTFKLADDT AREALDRMEA ERKKRGIPEE
AIRVLLYGET LRYPKLKPSD TSSR
//
