ID A0A244EEW4_9BURK Unreviewed; 292 AA.
AC A0A244EEW4;
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, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN ORFNames=A8M77_08640 {ECO:0000313|EMBL:OUM02999.1};
OS Variovorax sp. JS1663.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1851577 {ECO:0000313|EMBL:OUM02999.1, ECO:0000313|Proteomes:UP000195166};
RN [1] {ECO:0000313|EMBL:OUM02999.1, ECO:0000313|Proteomes:UP000195166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1663 {ECO:0000313|EMBL:OUM02999.1};
RX PubMed=28526789;
RA Mahan K.M., Zheng H., Fida T.T., Parry R.J., Graham D.E., Spain J.C.;
RT "A novel, iron-dependent enzyme that catalyzes the initial step in the
RT biodegradation of N-nitroglycine by Variovorax sp. strain JS1663.";
RL Appl. Environ. Microbiol. 83:0-0(2017).
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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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:OUM02999.1}.
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DR EMBL; LYMK01000007; OUM02999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A244EEW4; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000195166; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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; IPR023650; Beta-lactam_class-A_AS.
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; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Reference proteome {ECO:0000313|Proteomes:UP000195166};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..292
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012647880"
FT DOMAIN 45..262
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 292 AA; 30641 MW; 1E029E0986BB3C16 CRC64;
MHRRQFNSGL LLSLAALPFH LRAADANAFG GRLAEIEKAS GGRLGVAVLD SGSGRLAGHR
QDERFPLCST FKALAAALVL ARVDRGQETL ERRVRYARDE LVTYSPATEK HAGEDGMTMA
QLCEAAVTLS DNTAGNLMLA SFGGPAGLTA FMRSIGDAHT RLDRIETALN EARAGDARDT
TTPAAMAANM QKILLGGVLS PASRAQLMQW LDDNKTGDQR IRAGLPAGWR VGDKTGSGEN
GTANDVAILR PPGRAPVLLS VYLTATRAPM AERNATIAAV GAAAAAWISP GA
//
