ID A0A1E3LV03_9SPHN Unreviewed; 342 AA.
AC A0A1E3LV03;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=BFL28_17025 {ECO:0000313|EMBL:ODP37607.1};
OS Sphingomonas turrisvirgatae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1888892 {ECO:0000313|EMBL:ODP37607.1, ECO:0000313|Proteomes:UP000094487};
RN [1] {ECO:0000313|EMBL:ODP37607.1, ECO:0000313|Proteomes:UP000094487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCT13 {ECO:0000313|EMBL:ODP37607.1,
RC ECO:0000313|Proteomes:UP000094487};
RA D'Andrea M.M., Rossolini G.M., Thaller M.C.;
RT "Draft genome of the agarase producing Sphingomonas sp. MCT13.";
RL Submitted (AUG-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:ODP37607.1}.
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; MDDS01000026; ODP37607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3LV03; -.
DR STRING; 1888892.BFL28_17025; -.
DR Proteomes; UP000094487; 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.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Hydrolase {ECO:0000313|EMBL:ODP37607.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094487}.
FT DOMAIN 56..315
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 342 AA; 36579 MW; E78526DABF7350D5 CRC64;
MIGAGVHGDD LPAGLAAPTY RVAVPPTPRP LPVFPAPATL SSTVTSLARD FGGVVGISVR
SIDWGWQIDA NGNRRMPQQS VSKLWVAMTV LDARDKGRLT LDDPVTLTRE NLTLFHQPIA
ALVVKDGVYR TTVRELLLRA MQQSDNTAND RLLTLVGGPE AVRAFIRERQ LGQIRFGPGE
RLLQAGTAGL TWQQRYSMAG EFQRARAALP PTVRRAAFNA YVADPVDGAA PSAIALALAR
LKAGELLSPS STHFLTTVMS GTRTGRARLK AAVPPGWSLA HKTGTGQDLG SRTAGFNDIG
ILTAPDGKSY TLAVMIGDTA RVPRDRQLLM QAVVTAIVAN HR
//
