ID A0A1P8R451_9GAMM Unreviewed; 372 AA.
AC A0A1P8R451;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=BWR19_10715 {ECO:0000313|EMBL:APX93361.1};
OS Halomonas sp. 1513.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1883416 {ECO:0000313|EMBL:APX93361.1, ECO:0000313|Proteomes:UP000187327};
RN [1] {ECO:0000313|Proteomes:UP000187327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1513 {ECO:0000313|Proteomes:UP000187327};
RA Shuang W.;
RT "Complete genome sequence of Haloterrigena daqingensis type strain
RT (JX313T).";
RL Submitted (JAN-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; CP019326; APX93361.1; -; Genomic_DNA.
DR RefSeq; WP_076748229.1; NZ_CP019326.1.
DR AlphaFoldDB; A0A1P8R451; -.
DR STRING; 1883416.BWR19_10715; -.
DR KEGG; halo:BWR19_10715; -.
DR Proteomes; UP000187327; Chromosome.
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; 2.
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:APX93361.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187327};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..372
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012230477"
FT DOMAIN 57..165
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT DOMAIN 218..338
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 372 AA; 40439 MW; 0712FAC6A812D161 CRC64;
MIYRAICCLM LLLVSSALHA AGMHADWYYQ VDKRSAWQAP LETRLAELER DFSGEFGVYV
QDLHSGEALS WRADRDWYLA SLIKVPVAVE AFARLDQGEL SLDERLTLTR SDYVDGAGQT
NWQEPGSRLT LRFLLDEMLT VSDNTASDML IRRVGLAASN RRARDMVAAA GGDPAQLGEI
TSLLEVRHAL FGELHPDARD LGGMDYIALR HNDDLATRVT AFAERLGVAR EELKLDTYDA
AFDAYEASAL NGGTLVAFGE LLATLARGGP SQAGLSAASR EALLAVMRRT RSGEARLKAG
FGDDVVYAHK TGTQHRRTCD AGIAQRGGQR QVAVVACTRG PLDVVPHERL LAEVGAAIEA
SGVLSLPVPF IE
//
