ID I0SBB7_STRAP Unreviewed; 351 AA.
AC I0SBB7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=HMPREF1043_1661 {ECO:0000313|EMBL:EID20670.1};
OS Streptococcus anginosus subsp. whileyi CCUG 39159.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1095729 {ECO:0000313|EMBL:EID20670.1, ECO:0000313|Proteomes:UP000003245};
RN [1] {ECO:0000313|EMBL:EID20670.1, ECO:0000313|Proteomes:UP000003245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 39159 {ECO:0000313|EMBL:EID20670.1,
RC ECO:0000313|Proteomes:UP000003245};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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:EID20670.1}.
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DR EMBL; AICP01000048; EID20670.1; -; Genomic_DNA.
DR AlphaFoldDB; I0SBB7; -.
DR PATRIC; fig|1095729.3.peg.1755; -.
DR Proteomes; UP000003245; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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};
KW Carboxypeptidase {ECO:0000313|EMBL:EID20670.1};
KW Hydrolase {ECO:0000313|EMBL:EID20670.1};
KW Protease {ECO:0000313|EMBL:EID20670.1}.
FT DOMAIN 115..314
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 40..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 351 AA; 39918 MW; 1CAC96FA57F6F112 CRC64;
MSRKTMILCL IGCFIMCGVL VSSAVYFGQA RKAHPTKVAA NYPTSQEKPK NSSKESKLVT
RVSSKSIEEK QKVMESDLPV MEAYGLYYDY ANLNLVQVVK AYLDEMGIEH SQVAFSYKDS
TSGQTYAMNE TQPMTAGSTY KLPLNMLVVD EVEKGNLSLT ERFDITHTRY EYIGEHNNYV
AAFNGTMNIP EMQEYSLLYS ENTPAYALAE RLGGLDKAYT MYQRYGKGKG EIKTINQQNQ
TTTDYYIQVL DYLWKHQEKY KDILYYIGES FPNEYYKRYV RDIPIYQKPG YVAEALNVDA
VVCEEKPYLI ALYTAGLGGT TSESDEISGV GITQVGQLAY VINEWHRVNM N
//
