ID   A0A1H5QZF9_9PSEU        Unreviewed;       332 AA.
AC   A0A1H5QZF9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=SAMN05421837_105765 {ECO:0000313|EMBL:SEF31500.1};
OS   Amycolatopsis pretoriensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=218821 {ECO:0000313|EMBL:SEF31500.1, ECO:0000313|Proteomes:UP000198878};
RN   [1] {ECO:0000313|EMBL:SEF31500.1, ECO:0000313|Proteomes:UP000198878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44654 {ECO:0000313|EMBL:SEF31500.1,
RC   ECO:0000313|Proteomes:UP000198878};
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; FNUJ01000005; SEF31500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5QZF9; -.
DR   STRING; 218821.SAMN05421837_105765; -.
DR   Proteomes; UP000198878; 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..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..332
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011433980"
FT   DOMAIN          72..278
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   332 AA;  35253 MW;  3E40DAE7DAD55486 CRC64;
     MGYRLNRRAA FGVGTAVVAG SVLTGSPAFA QEADIEASPA TPDRARQKVK RVYDDAAAEA
     GGTWNSYISV ADQVAVDVAS DEVVEAYSVN KVAVAVTLMD KIDRGLLTLD QQVQVPESIV
     VPGGDGIIIL DKAYPSAFTL GHVLSLFLTV SDDTCVRLVG LVVPAAEINQ ILVSKGFPKT
     QVTPVANPNR YFLGQTTPRE THDLLKALVA GTLLSPASTE YLLSILRSQV AFTDGIRREM
     SSADRARIAT KAGWLNDGRN EAGIMFDAAG KPVVIYSMFA HGQANPDDFG ATHPVRQASA
     KMGPKFLRAV DKIAGAGTKA FRAPAYRQYN GG
//