ID   BLA1_ACTPL              Reviewed;         305 AA.
AC   P67920; P33949;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Beta-lactamase ROB-1;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=rob1; Synonyms=bla;
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OG   Plasmid RRob.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1455627; DOI=10.1016/0378-1135(92)90154-l;
RA   Chang Y.-F., Shi J., Shin S.J., Lein D.H.;
RT   "Sequence analysis of the ROB-1 beta-lactamase gene from Actinobacillus
RT   pleuropneumoniae.";
RL   Vet. Microbiol. 32:319-325(1992).
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10101};
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; S51028; AAB24384.1; -; Genomic_DNA.
DR   PIR; A57002; A57002.
DR   RefSeq; WP_005618523.1; NZ_MK203847.1.
DR   RefSeq; YP_001941143.1; NC_010795.1.
DR   AlphaFoldDB; P67920; -.
DR   SMR; P67920; -.
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; -; 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; PTHR35333; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..305
FT                   /note="Beta-lactamase ROB-1"
FT                   /id="PRO_0000017039"
FT   ACT_SITE        86
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         248..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  33869 MW;  6146E12B76607422 CRC64;
     MLNKLKIGTL LLLTLTACSP NSVHSVTSNP QPASAPVQQS ATQATFQQTL ANLEQQYQAR
     IGVYVWDTET GHSLSYRADE RFAYASTFKA LLAGAVLQSL PEKDLNRTIS YSQKDLVSYS
     PETQKYVGKG MTIAQLCEAA VRFSDNSATN LLLKELGGVE QYQRILRQLG DNVTHTNRLE
     PDLNQAKPND IRDTSTPKQM AMNLNAYLLG NTLTESQKTI LWNWLDNNAT GNPLIRAATP
     TSWKVYDKSG AGKYGVRNDI AVVRIPNRKP IVMAIMSTQF TEEAKFNNKL VEDAAKQVFH
     TLQLN