ID   A0A1I6D160_9PSEU        Unreviewed;       466 AA.
AC   A0A1I6D160;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=SAMN04488564_101783 {ECO:0000313|EMBL:SFQ99110.1};
OS   Lentzea waywayandensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=84724 {ECO:0000313|EMBL:SFQ99110.1, ECO:0000313|Proteomes:UP000198583};
RN   [1] {ECO:0000313|EMBL:SFQ99110.1, ECO:0000313|Proteomes:UP000198583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44232 {ECO:0000313|EMBL:SFQ99110.1,
RC   ECO:0000313|Proteomes:UP000198583};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOYL01000001; SFQ99110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6D160; -.
DR   STRING; 84724.SAMN04488564_101783; -.
DR   OrthoDB; 3501904at2; -.
DR   Proteomes; UP000198583; Unassembled WGS sequence.
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; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..466
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011521970"
FT   DOMAIN          176..294
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   466 AA;  50691 MW;  090A3F5C662E97CD CRC64;
     MKLKRFAVLG TVVALAGATL APAASADEYH RPLADRLREA IVAQNFKDVI DLTPPELVAR
     SAGKREKYDA SPAELMNKAQ ARMAAAAGKP LHQTPNMDAA IIELDPFGRP KSVANVLLSP
     QYPNGVVVPV THQGLSTDQV RYRWWDDTEW DVNGGKGTVD VLPGRENAAI DFSSPYPASV
     LKLMVGFGVL RLADQGKIDL DADYVYAPDP VRPACGGPSV KKIRQHFDEM ITKSQNESTC
     SLIKLIHDHN AWDAVNQTFV DLGMPTLMVT GTLPGNGGRW IGSNMSGLDT AKLLLLVNGG
     AGVLWTTDKG KPVTRNELSY SSRKFFQETL AGQGHNEMLS TPNWCGRDYP TQGIPQQVPS
     RWIKPDGTVT VGDAVYDRDV RPCNDAAEVT FAHKTGWVDT TGSDAGIVKS LRGKDNRNYI
     VVVFCNLGTD YVDADRPADP PGVYPVLYTQ KYAQLGKAID TIMKNL
//