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Database: UniProt
Entry: A0A1R0XMK0_9BACL
LinkDB: A0A1R0XMK0_9BACL
Original site: A0A1R0XMK0_9BACL 
ID   A0A1R0XMK0_9BACL        Unreviewed;       227 AA.
AC   A0A1R0XMK0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=UPF0173 metal-dependent hydrolase BSO21_07565 {ECO:0000256|HAMAP-Rule:MF_00457};
GN   ORFNames=BSO21_07565 {ECO:0000313|EMBL:OMD36259.1};
OS   Paenibacillus odorifer.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=189426 {ECO:0000313|EMBL:OMD36259.1, ECO:0000313|Proteomes:UP000187158};
RN   [1] {ECO:0000313|EMBL:OMD36259.1, ECO:0000313|Proteomes:UP000187158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0433 {ECO:0000313|EMBL:OMD36259.1,
RC   ECO:0000313|Proteomes:UP000187158};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
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}.
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:OMD36259.1}.
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DR   EMBL; MPVP01000029; OMD36259.1; -; Genomic_DNA.
DR   RefSeq; WP_076218346.1; NZ_MPVP01000029.1.
DR   AlphaFoldDB; A0A1R0XMK0; -.
DR   STRING; 189426.PODO_04850; -.
DR   eggNOG; COG2220; Bacteria.
DR   Proteomes; UP000187158; 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; PF13483; Lactamase_B_3; 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, ECO:0000313|EMBL:OMD36259.1}.
FT   DOMAIN          7..191
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   227 AA;  24469 MW;  3951B8C87345E727 CRC64;
     MKITYYGHSA LLVETGNVKV IIDPFLSGNP NSGISPANIS VDAVLLTHGH SDHFGDAVEI
     AKQNDCPIFA VFELAEYCRM KGAQVKHMNI GGSHTYAGMT VKFTQAFHSS SIQEGDSWIY
     AGQPAGILLT IEGKTIFHAG DTALFSDLRL IGERNAIALA ALPIGDMLTM GPDDALLAAR
     WLRADKVIPL HYNTFPDIAQ DGADFCDRLH QEGVEGFPLK AGESVEI
//
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