BLA1_HAEIF
ID BLA1_HAEIF Reviewed; 305 AA.
AC P67918; 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 Haemophilus influenzae.
OG Plasmid RRob.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F990; PLASMID=RRob;
RX PubMed=2201253; DOI=10.1128/aac.34.7.1354;
RA Juteau J.-M., Levesque R.C.;
RT "Sequence analysis and evolutionary perspectives of ROB-1 beta-lactamase.";
RL Antimicrob. Agents Chemother. 34:1354-1359(1990).
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}.
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; AF022114; AAB72007.1; -; Genomic_DNA.
DR PIR; A60680; A60680.
DR RefSeq; WP_005618523.1; NZ_NECE01000071.1.
DR RefSeq; YP_004074575.1; NC_014813.1.
DR RefSeq; YP_006959620.1; NC_019174.1.
DR RefSeq; YP_006959624.1; NC_019175.1.
DR RefSeq; YP_006959628.1; NC_019176.1.
DR RefSeq; YP_006959632.1; NC_019177.1.
DR RefSeq; YP_006959636.1; NC_019178.1.
DR AlphaFoldDB; P67918; -.
DR SMR; P67918; -.
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_0000017040"
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