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Database: UniProt
Entry: A0A239BGQ3_9ACTN
LinkDB: A0A239BGQ3_9ACTN
Original site: A0A239BGQ3_9ACTN 
ID   A0A239BGQ3_9ACTN        Unreviewed;       455 AA.
AC   A0A239BGQ3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=SAMN05216276_1003170 {ECO:0000313|EMBL:SNS06538.1};
OS   Streptosporangium subroseum.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=106412 {ECO:0000313|EMBL:SNS06538.1, ECO:0000313|Proteomes:UP000198282};
RN   [1] {ECO:0000313|EMBL:SNS06538.1, ECO:0000313|Proteomes:UP000198282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2132 {ECO:0000313|EMBL:SNS06538.1,
RC   ECO:0000313|Proteomes:UP000198282};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZOD01000003; SNS06538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239BGQ3; -.
DR   OrthoDB; 108135at2; -.
DR   Proteomes; UP000198282; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000198282};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..455
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038795533"
FT   DOMAIN          46..135
FT                   /note="ORF 12 gene product N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18042"
FT   DOMAIN          186..287
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   455 AA;  49164 MW;  90F0B26DCA13EC6D CRC64;
     MRLPFRSTRF LTLAVVTAAV PFTSLAGGGQ PATASTAQVV TVAPEIPDSP AGRQLRWFLD
     APSRAPLTES ELGEHVNAAY LQALTVDGFN AFLKNATGFQ LEELTTVTPT ALVGTGAIGS
     QKFVLQLRVD AAGKINLIGA TPPAPPIPAS PTSWKQLDTR LRKAAPQVGF LAAEIDSRGR
     CEVVHAVNPD RAQPLGSIFK LYVMGAVAEK IRDDRLSWNT KLTIRPEWRS TGEGGLAERP
     DNSTVTVREA AKLMISISDN TATDLLIHTV GRGAVESTVR RWSGHAKQNV PFLTTRELFL
     LKGVNYPGQA NAYLALRPAK KAAYLKNTVA KQALTDIRPW DRPREIDRLE WFGSPRDVCR
     AYAGLATLNS KPLHEAMSAD DLGLKLDPRK WPVVWAKGGS ELGVLDLSFR ARSAKEKTYV
     VTALTNNPQS AIDERTAVGE LISLSRGAFT LATSG
//
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