ID A0A172UU31_9MYCO Unreviewed; 435 AA.
AC A0A172UU31;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=A7U43_06410 {ECO:0000313|EMBL:ANE82692.1};
OS Mycobacterium adipatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1682113 {ECO:0000313|EMBL:ANE82692.1, ECO:0000313|Proteomes:UP000077143};
RN [1] {ECO:0000313|EMBL:ANE82692.1, ECO:0000313|Proteomes:UP000077143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC-RL4 {ECO:0000313|EMBL:ANE82692.1,
RC ECO:0000313|Proteomes:UP000077143};
RA Ren L., Fan S., Ruth N., Jia Y., Wang J., Qiao C.;
RT "Complete genome sequence of a phthalic acid esters degrading Mycobacterium
RT sp. YC-RL4.";
RL Submitted (MAY-2016) 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; CP015596; ANE82692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A172UU31; -.
DR STRING; 1682113.A7U43_06410; -.
DR KEGG; madi:A7U43_06410; -.
DR Proteomes; UP000077143; 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 Gene3D; 1.10.8.620; ORF12 helical bundle domain-like; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR040846; ORF_12_N.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR Pfam; PF18042; ORF_12_N; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Hydrolase {ECO:0000313|EMBL:ANE82692.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077143};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..435
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039628465"
FT DOMAIN 33..120
FT /note="ORF 12 gene product N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18042"
FT DOMAIN 165..266
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 435 AA; 46732 MW; 65E80DD64752D9D5 CRC64;
MTALATAAVL LATGCAHTGP PVAEAAYGMH IDTNTPQGLR AKQLLDMVNS DWPIGTVTVG
TLAIPGMIEP VGAAMDRLWA DRPITVTAIS LGAGQATLHV RNSYDVGQTI HLRTSDDGLV
DRFEVDIDRP EIGQWSDIDA AIRESGADYA YQVSKVSGGA CTTVAGTDVD RSMPLASIFK
LYVLLAVAEA VNAGTLTWHE QLTITEANKA VGSAGFNDLE PGARVSVKDA AQQMISASDN
MATDMLMARL GPAALQHALR TAGHHDPASM TPFPSTYELF AIGWGKPDVR EEWKTATRAH
RAEMLAHTRA VPYEPDPMLN RTPASPYGIE WYGTPMDVCR VHAALQVAAH GPAAPVRQIL
SATPGIELDR AKWRYIGAKG GNLPGDLTFS WYAEDRDGQG WVVSYQLTWP RYRSLTAATW
LQSIAMQSFG LIPAT
//
