ID   A0A069I8A9_9BURK        Unreviewed;       300 AA.
AC   A0A069I8A9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, 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=CF70_016075 {ECO:0000313|EMBL:KDP85024.1};
OS   Cupriavidus sp. SK-3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP85024.1, ECO:0000313|Proteomes:UP000023560};
RN   [1] {ECO:0000313|EMBL:KDP85024.1, ECO:0000313|Proteomes:UP000023560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-3 {ECO:0000313|EMBL:KDP85024.1,
RC   ECO:0000313|Proteomes:UP000023560};
RA   Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT   "Cupriavidus sp. strain SK-3.";
RL   Submitted (MAY-2014) 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:KDP85024.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JFJV02000234; KDP85024.1; -; Genomic_DNA.
DR   RefSeq; WP_035870551.1; NZ_JFJV02000234.1.
DR   AlphaFoldDB; A0A069I8A9; -.
DR   OrthoDB; 9784149at2; -.
DR   Proteomes; UP000023560; Unassembled WGS sequence.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
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   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..300
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001661994"
FT   DOMAIN          52..268
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   300 AA;  31119 MW;  6A7E7507E09856A5 CRC64;
     MRHSPVRRTL LLAAASVPFT SACTSWAGRA GGSAAAQDRL AALESAAGGR LGVAALNTAS
     GARISHRASE RFALCSTFKV LAASAILQRS AAESGLLQRR IAYTKDELVA YSPVTGKHTG
     DGMTVSELCA AALQYSDNTA ANLLMKILGG PAAVTAFARS IGDDAFRLDR WETELNTAIP
     GDPRDTSTPA AMSRSLQRLA LGDALGAAER GRLVAWMRGN TTGATRIRAG VPADWQVADK
     TGSGDYGAAN DIAVAWPPGK PPVVMAIYFT QGDKDAAYRN DVLATAARIV AETIGQAGMA
//