ID A1A306_BIFAA Unreviewed; 357 AA.
AC A1A306;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN OrderedLocusNames=BAD_1308 {ECO:0000313|EMBL:BAF40089.1};
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF40089.1, ECO:0000313|Proteomes:UP000008702};
RN [1] {ECO:0000313|EMBL:BAF40089.1, ECO:0000313|Proteomes:UP000008702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
RC {ECO:0000313|Proteomes:UP000008702};
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) 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}.
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DR EMBL; AP009256; BAF40089.1; -; Genomic_DNA.
DR AlphaFoldDB; A1A306; -.
DR STRING; 367928.BAD_1308; -.
DR KEGG; bad:BAD_1308; -.
DR HOGENOM; CLU_031960_2_0_11; -.
DR Proteomes; UP000008702; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008702};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 142..187
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT DOMAIN 189..331
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 62..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 357 AA; 37481 MW; 242238EF17486D2D CRC64;
MGRHSNYPRW ASEQSRAAFD GRRRITVAVI AAVCVVAVAL AGCAIAIAGA RRHGAASSAA
AVAKTETPAV KGADGSAKSA EPNEPTKPAT RGETAAEHTA LDRKQTPKAD ERKTQTAERQ
TLLAALQSQL SGKTAQYQGS WQVYVEDLDS GATAVVNSHQ SYSASVVKLM VMLAVFQKVS
EGTLAEDASL DGLLEQMITV SSNEATNALV ERLGSGNINA GFGVVNSVAA QYGFNESHLN
SRMGDLSNYS TKQTSVADQG RFLAAAYRGQ LVSAGYSKRM TDIMSRQTRR AKIPAGLPQG
VACANKTGEA PGVENDSAIV YGEHPYVIAV MSSDVPDSSA AQAQIRDISS TVWASLQ
//
