ID E3E6U9_PAEPS Unreviewed; 336 AA.
AC E3E6U9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Beta-lactamase {ECO:0000313|EMBL:ADO58501.1};
GN Name=romA {ECO:0000313|EMBL:ADO58501.1};
GN ORFNames=PPSC2_21350 {ECO:0000313|EMBL:ADO58501.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO58501.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO58501.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO58501.1,
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};
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DR EMBL; CP002213; ADO58501.1; -; Genomic_DNA.
DR RefSeq; WP_013373069.1; NC_014622.2.
DR AlphaFoldDB; E3E6U9; -.
DR STRING; 1406.LK13_08575; -.
DR KEGG; ppm:PPSC2_21350; -.
DR PATRIC; fig|886882.15.peg.4538; -.
DR eggNOG; COG2220; Bacteria.
DR HOGENOM; CLU_020884_1_0_9; -.
DR OrthoDB; 9805728at2; -.
DR Proteomes; UP000006868; Chromosome.
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; 2.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT DOMAIN 74..286
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
SQ SEQUENCE 336 AA; 38759 MW; F88C675DCC2DE442 CRC64;
MPKVRFNNMD HVNTDKTIKQ FRQWRQERRS KIKDYTFVVP NHPPELEFLH HNREMATATW
VGHSTFFIQY LGLNIVTDPV WAERMAFDKR LAPPGIRIQD VPPLDIILLS HSHYDHLHLA
SLRKLYRADT LMLVPSGLKS KMIRKGFRNC HELQWWEHFT VGGVRITFVP AQHWTRRTPF
DTNTSHWGGY VLQSEQQVTG SATSVAGSDA HAESDSTEAP TLYFVGDTGY FRGFKEIGER
FAIDLTFMPI GAYEPEWFMT SQHVTPEEAL QGFVDCGADQ MIPMHYGAFK LADDTPREAL
DRLEVERERL GIAKERIHVL GHGETLKIGR RCSTRI
//
