ID Q0STN3_CLOPS Unreviewed; 259 AA.
AC Q0STN3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN OrderedLocusNames=CPR_1202 {ECO:0000313|EMBL:ABG85703.1};
OS Clostridium perfringens (strain SM101 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=289380 {ECO:0000313|EMBL:ABG85703.1, ECO:0000313|Proteomes:UP000001824};
RN [1] {ECO:0000313|EMBL:ABG85703.1, ECO:0000313|Proteomes:UP000001824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM101 / Type A {ECO:0000313|Proteomes:UP000001824};
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., Deboy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000256|ARBA:ARBA00001526};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009}.
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DR EMBL; CP000312; ABG85703.1; -; Genomic_DNA.
DR RefSeq; WP_003456515.1; NC_008262.1.
DR AlphaFoldDB; Q0STN3; -.
DR GeneID; 69449082; -.
DR KEGG; cpr:CPR_1202; -.
DR BioCyc; CPER289380:GI76-1218-MONOMER; -.
DR Proteomes; UP000001824; Chromosome.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251}.
FT DOMAIN 16..229
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 259 AA; 29312 MW; 2DA1EE63CD02D400 CRC64;
MKEVQKYLES RIGSYSFFFE DLKSGYTYGY NENVKMISAG CMKLPIAIAL IKEVEEGKID
FLDKVKIESS DKVYGTGIIH EFGERDYTVF ELMVAMLIQS DNTAANKIID LVGMDKINET
IKEFGMKNTE LNRKTADERN FKSDVENYTT AYDLTLAWKK LSEGSFLSKE NSQMLIDILT
RQQIKNKLAL YIPDNLKFDI SSKTGDKKGV ENDTALIHTQ KGNFACTVMS SGIPNSVYGT
VTLAKSGKMT WDAIMNNWH
//
