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Database: UniProt
Entry: A0A1V4LWX9_9PSED
LinkDB: A0A1V4LWX9_9PSED
Original site: A0A1V4LWX9_9PSED 
ID   A0A1V4LWX9_9PSED        Unreviewed;       305 AA.
AC   A0A1V4LWX9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=BZ163_02200 {ECO:0000313|EMBL:OPK11770.1};
OS   Pseudomonas sp. VI4.1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1941346 {ECO:0000313|EMBL:OPK11770.1, ECO:0000313|Proteomes:UP000189889};
RN   [1] {ECO:0000313|EMBL:OPK11770.1, ECO:0000313|Proteomes:UP000189889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VI4.1 {ECO:0000313|EMBL:OPK11770.1,
RC   ECO:0000313|Proteomes:UP000189889};
RA   Imperato V., Thijs S., Mcammond B., Douwen Y., Broeders P., Kowalkowski L.,
RA   Gawronski S., Vangronsveld J.;
RT   "Draft genome sequence of Pseudomonas yorbenii VI4.1, a hydrocarbonoclastic
RT   isolate from crude oil contaminated soil in Bobrka, Poland.";
RL   Submitted (FEB-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}.
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:OPK11770.1}.
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DR   EMBL; MULM01000071; OPK11770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4LWX9; -.
DR   Proteomes; UP000189889; 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; 3.40.710.10; 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   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251}.
FT   DOMAIN          40..264
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   305 AA;  33600 MW;  FE9C6032DF7A8A65 CRC64;
     MRVEPEVQDW LASGGWPLHI IGQQMIERAQ LKPACSYRWC IHDVVRGTRH AFNEHARVPA
     SSTRKLYILV AVLLLIEHGE LALSDSVVVD NQKAGAQTCG GLWLLDSPRV FTVAELLKLM
     MGLSDNIATF YLVDLLGLER LNALSTVVGL SGTWHLSAVP SQALTADHPL SAVNTTTASD
     LVTALSILVE GANSRLPAGG AFIRRELCEF GLNSMRAQQD TTAIRSWLTD VDQVGDKHGI
     GYRNYNNVAY LAHGGGVRII FSIIVDDLHR IESPMPAFAH ARDFIALFSR LLDDYTRLEY
     PSKEL
//
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