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Database: UniProt
Entry: C8C173_9ZZZZ
LinkDB: C8C173_9ZZZZ
Original site: C8C173_9ZZZZ 
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
//
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