ID E3EBC4_PAEPS Unreviewed; 209 AA.
AC E3EBC4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Metal-binding protein {ECO:0000313|EMBL:ADO58456.1};
GN Name=glxII {ECO:0000313|EMBL:ADO58456.1};
GN ORFNames=PPSC2_21135 {ECO:0000313|EMBL:ADO58456.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO58456.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO58456.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO58456.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP002213; ADO58456.1; -; Genomic_DNA.
DR RefSeq; WP_013373025.1; NC_014622.2.
DR AlphaFoldDB; E3EBC4; -.
DR STRING; 1406.LK13_08365; -.
DR KEGG; ppm:PPSC2_21135; -.
DR PATRIC; fig|886882.15.peg.4493; -.
DR eggNOG; COG0491; Bacteria.
DR HOGENOM; CLU_030571_5_2_9; -.
DR OrthoDB; 9802248at2; -.
DR Proteomes; UP000006868; Chromosome.
DR CDD; cd06262; metallo-hydrolase-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; PTHR46233; HYDROXYACYLGLUTATHIONE HYDROLASE GLOC; 1.
DR PANTHER; PTHR46233:SF3; HYDROXYACYLGLUTATHIONE HYDROLASE GLOC; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT DOMAIN 14..192
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 209 AA; 22812 MW; 837716B68EB99A6C CRC64;
MTLSIRSFNL GPLQTNAYLL QGDDPQRAVI IDPGMNPGPL LRAIESLTIE AILLTHAHFD
HIGGVEEIRN AKGCPVYLHA LEQDWLTSPK LNGSLMWPEA SPPISTGPAE YDLAEGQQLK
LIGHTFKVLH TPGHSPGSVS FLCGKDLFSG DVLFRQGVGR TDLTGGRERD LYDSIQNKLF
PLGDDVTVYP GHGPKTSIGY EKANNPYIR
//
