ID A0A1A3PHS8_9MYCO Unreviewed; 453 AA.
AC A0A1A3PHS8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
DE AltName: Full=Penicillinase {ECO:0000256|ARBA:ARBA00030171};
GN ORFNames=A5658_13720 {ECO:0000313|EMBL:OBK33285.1};
OS Mycobacterium sp. 1245111.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834073 {ECO:0000313|EMBL:OBK33285.1, ECO:0000313|Proteomes:UP000092232};
RN [1] {ECO:0000313|EMBL:OBK33285.1, ECO:0000313|Proteomes:UP000092232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1245111.1 {ECO:0000313|EMBL:OBK33285.1,
RC ECO:0000313|Proteomes:UP000092232};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
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:OBK33285.1}.
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DR EMBL; LZLV01000145; OBK33285.1; -; Genomic_DNA.
DR RefSeq; WP_067340929.1; NZ_LZLV01000145.1.
DR AlphaFoldDB; A0A1A3PHS8; -.
DR STRING; 1834073.A5658_13720; -.
DR Proteomes; UP000092232; Unassembled WGS sequence.
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; 3.10.450.280; -; 1.
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; IPR040846; ORF_12_N.
DR InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Hydrolase {ECO:0000313|EMBL:OBK33285.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..453
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039407445"
FT DOMAIN 53..138
FT /note="ORF 12 gene product N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18042"
FT DOMAIN 182..286
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 453 AA; 49006 MW; 795BD4359BCED33E CRC64;
MPDLASKPRR RSRLRRVAAL AASALLVALT PGCAPPRAPS ANAAGSGRQI DMRTPAGLRA
QQTLDMLNSD WPIGPVGVGT LAAPKMATQI QTMMEKLWWD RPFTLHGVDI KAGAATLQLT
TSYGAEQEIR IHTNDDTLVD GFDLTTLPPK ISSWNDVDAV LGKTKARYSW QATKVVDGHC
DRVAGTNTDM SLPLASIFKL YVLYAVSDAI KVGTVSWDDQ LTVTEKGRAV GSSMDLPVGA
QISVRTAAEK MIATSDNMAT DMLIERVGPQ AVDAALAAAG HHDPAAMTPF PTMYELFTVA
WGRPDLREQW KHGSPADRAE MLQRANSATY QPDPFRAHVP ASESGAEWYG NADDICRVHV
ALQAGAVGPA APVKKILDAA TGINFDRNEW PYIAAKAGGL PGDLTFSWYA LDKTRQPWVV
SFQLNWPRDH GPAITGWVLQ IAKQVFALLP TQH
//
