ID A0PV37_MYCUA Unreviewed; 437 AA.
AC A0PV37;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN Name=lpqF {ECO:0000313|EMBL:ABL06206.1};
GN OrderedLocusNames=MUL_4168 {ECO:0000313|EMBL:ABL06206.1};
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL06206.1, ECO:0000313|Proteomes:UP000000765};
RN [1] {ECO:0000313|EMBL:ABL06206.1, ECO:0000313|Proteomes:UP000000765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99 {ECO:0000313|EMBL:ABL06206.1,
RC ECO:0000313|Proteomes:UP000000765};
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000325; ABL06206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0PV37; -.
DR KEGG; mul:MUL_4168; -.
DR eggNOG; COG2367; Bacteria.
DR HOGENOM; CLU_042385_1_0_11; -.
DR Proteomes; UP000000765; Chromosome.
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; 3.10.450.280; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 1.10.8.620; ORF12 helical bundle domain-like; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR040846; ORF_12_N.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR Pfam; PF18042; ORF_12_N; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Lipoprotein {ECO:0000313|EMBL:ABL06206.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..437
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002628575"
FT DOMAIN 37..122
FT /note="ORF 12 gene product N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18042"
FT DOMAIN 167..268
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 437 AA; 46931 MW; 36E87665724F922F CRC64;
MLTAAAALVL TLTPGCSSSP TPSANAANPQ RRIDTVTPPG LRAQQTMDML NSDWPIGPAG
VATLAAPSKV DSVEATMEGL WWDRPFALDS VDISASVATL HLTSSYGARQ DIRLHTDDGG
WVDRFELATL PPPTITAWRD VDAVLSKTGA RYSYQVSKVE KGQCTRVAGT NTNQPLPLAS
IFKLYVLHAL ADAIKSGTAS WDDQLTVTAK SKAVGSSGLE LSPGDHVSVR RAAEKMIANS
DNMATDLLIG RLGKHAIEQA LATAGHHDPA SMTPFPTMYE LFSVGWGQPD LREQWKQASA
QQRAALLEQA DSTPYRPDPT RAHTPASNYG AEWYGSAEDI CRVHLALQAD AVGPAAPVRK
ILSAVAGIAL DRNYWPYIGA KAGGLPGDLT FSWYAEDKTG QPWVVSFQLN WPRDHGPNVT
GWMLQVAKQV FALVAPE
//
