ID C8C173_9ZZZZ Unreviewed; 291 AA.
AC C8C173;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
OS uncultured organism.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=155900 {ECO:0000313|EMBL:ACT97656.1};
RN [1] {ECO:0000313|EMBL:ACT97656.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19713526; DOI=10.1126/science.1176950;
RA Sommer M.O., Dantas G., Church G.M.;
RT "Functional characterization of the antibiotic resistance reservoir in the
RT human microflora.";
RL Science 325:1128-1131(2009).
RN [2] {ECO:0000313|EMBL:ACT97656.1}
RP NUCLEOTIDE SEQUENCE.
RA Sommer M.O.A., Dantas G., Church G.;
RL Submitted (JUL-2009) 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; GQ343169; ACT97656.1; -; Genomic_DNA.
DR AlphaFoldDB; C8C173; -.
DR SMR; C8C173; -.
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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 50..264
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 291 AA; 31144 MW; 49C531A7D5607BA4 CRC64;
MVKKSLRQFT LMATATVTLL LGSVPLYAQT ADVQQKLAEL ERQSGGRLGV ALINTADNSQ
ILYRADERFA MCSTSKVMAA AAVLKKSESE PNLLNQRVEI KKSDLVNYNP IAEKHVNGTM
SLAELSAAAL QYSDNVAMNK LIAHVGGPAS VTAFARQLGD ETFRLDRTEP TLNTAIPGDP
RDTTSPRAMA QTLRNLTLGK ALGDSQRAQL VTWMKGNTTG AASIQAGLPA SWVVGDKTGS
GGYGTTNDIA VIWPKDRAPL ILVTYFTQPQ PKAESRRDVL ASAAKIVTDG L
//