ID Q59830_STRCL Unreviewed; 332 AA.
AC Q59830;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN Name=bla {ECO:0000313|EMBL:CAA90895.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:CAA90895.1};
RN [1] {ECO:0000313|EMBL:CAA90895.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 3585 {ECO:0000313|EMBL:CAA90895.1};
RA Perez-Llarena F.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAA90895.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 3585 {ECO:0000313|EMBL:CAA90895.1};
RX PubMed=9324249;
RA Perez-Llarena F., Martin J.F., Galleni M., Coque J.J., Fuente J.L.,
RA Frere J.M., Liras P.;
RT "The bla gene of the cephamycin cluster of Streptomyces clavuligerus
RT encodes a class A beta-lactamase of low enzymatic activity.";
RL J. Bacteriol. 179:6035-6040(1997).
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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; Z54190; CAA90895.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59830; -.
DR SMR; Q59830; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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 InterPro; IPR023650; Beta-lactam_class-A_AS.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 72..286
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 28..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 35247 MW; 5516BE0AB6EB5151 CRC64;
MRAGAVRPSA VSRRALLTAA ALLPLAGCGT RERTGSPPAS VRAAGRGSPG AEGRARVADL
AALEREHGAR LGVYALETGT GAEVAHRADE RFAFCSTFKA LAAAAVLHHH PIRHLERRVT
WTRADVDSIS PVTEDHIATG LTVGQLCDAA IRHSDGTAGN LLMRDLGGPS RLTAYLRGLG
DSVSRMDQYE PELNHDPPHD PRDTTTPRAI ASDYRKLVLG DALTPDRRAL LTDWLVRNTT
GGRRIRAGVP SGWRVADKTG TGNYGRANDI AVLWPPRSSP LVVAVMSDRP GFRTPPSERL
IAEDRGAIVA GLVRHPPTHA SGAGAPSRHP GP
//
