ID A0A0B2BXX1_9SPHN Unreviewed; 346 AA.
AC A0A0B2BXX1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=PK98_13280 {ECO:0000313|EMBL:KHL24852.1};
OS Croceibacterium mercuriale.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL24852.1, ECO:0000313|Proteomes:UP000030988};
RN [1] {ECO:0000313|EMBL:KHL24852.1, ECO:0000313|Proteomes:UP000030988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coronado {ECO:0000313|EMBL:KHL24852.1,
RC ECO:0000313|Proteomes:UP000030988};
RA Coil D.A., Eisen J.A.;
RT "Draft genome sequence of Kirrobacter mercurialis.";
RL Submitted (NOV-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:KHL24852.1}.
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DR EMBL; JTDN01000002; KHL24852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2BXX1; -.
DR STRING; 1572751.PK98_13280; -.
DR MEROPS; S11.A01; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000030988; 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 Reference proteome {ECO:0000313|Proteomes:UP000030988};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..346
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002088276"
FT DOMAIN 81..306
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 346 AA; 36493 MW; 75BF6D9B92DA0355 CRC64;
MQIGTLARTA LAAALAFGGL AGGTAIARDA APPQGAVQLE AAFDTAFGTD IRSPRDYSAS
YEGILQQQIA RLADGGQGRI GLFAVDLATG EEIAVLGDQR FPMASTSKIA IAATFMEGVE
RGRWSLSSEF PLMVPVASRP FSTAVAPVRA GEHLSARQLI ELMITRSSNP ATDALLKAVG
GPAAVNDWVR RNGISEFNLS RDIATLVRDD GEVDPATSID TRDSATPRAM VQLLSGLHQG
RFLSDSSRRV ILGAMERCRT GTRRIRALMP AGVTVSHKTG TLNNTASDIG FIHAPDGRTI
AVAIYVTGQG GRPGRDAKIA NLARAIYDGY AQQGTLAARQ MVNANY
//
