ID BLAF_MYCFO Reviewed; 294 AA.
AC Q59517;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Beta-lactamase;
DE EC=3.5.2.6;
DE AltName: Full=Penicillinase;
DE Flags: Precursor;
GN Name=blaF;
OS Mycolicibacterium fortuitum (Mycobacterium fortuitum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1766;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8065266; DOI=10.1111/j.1365-2958.1994.tb01037.x;
RA Timm J.C.S., Perilli M.G., Duez C., Trias J., Orefici G., Fattorini L.,
RA Amicosante G., Oratore A., Joris B.;
RT "Transcription and expression analysis, using lacZ and phoA gene fusions,
RT of Mycobacterium fortuitum beta-lactamase genes cloned from a natural
RT isolate and a high-level beta-lactamase producer.";
RL Mol. Microbiol. 12:491-504(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC STRAIN=D316;
RA Sauvage E., Fonze E., Vermeire M., Galleni M., Quinting B., Frere J.-M.,
RA Charlier P.;
RT "The crystal structure of the class A beta-lactamase from Mycobacterium
RT fortuitum: structural basis for a broad substrate specificity.";
RL Submitted (SEP-1998) to the PDB data bank.
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 -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; L25634; AAA19882.1; -; Unassigned_DNA.
DR PIR; S49543; S49543.
DR RefSeq; WP_063842628.1; NG_047497.1.
DR PDB; 2CC1; X-ray; 2.13 A; A=33-294.
DR PDBsum; 2CC1; -.
DR AlphaFoldDB; Q59517; -.
DR SMR; Q59517; -.
DR STRING; 1766.XA26_25690; -.
DR BRENDA; 3.5.2.6; 3498.
DR EvolutionaryTrace; Q59517; -.
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; 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 InterPro; IPR023650; Beta-lactam_class-A_AS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase;
KW Signal.
FT SIGNAL 1..32
FT /note="Tat-type signal"
FT CHAIN 33..294
FT /note="Beta-lactamase"
FT /id="PRO_0000017003"
FT REGION 226..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /note="Acyl-ester intermediate"
FT BINDING 237..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VARIANT 82
FT /note="A -> S (in amoxcillin-resistant strain)"
FT VARIANT 116
FT /note="A -> E (in amoxcillin-resistant strain)"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:2CC1"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:2CC1"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2CC1"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:2CC1"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:2CC1"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:2CC1"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:2CC1"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:2CC1"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:2CC1"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:2CC1"
FT STRAND 259..271
FT /evidence="ECO:0007829|PDB:2CC1"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:2CC1"
SQ SEQUENCE 294 AA; 30951 MW; 87DE5D6333867B24 CRC64;
MTGLSRRNVL IGSLVAAAAV GAGVGGAAPA FAAPIDDQLA ELERRDNVLI GLYAANLQSG
RRITHRLDEM FAMCSTFKGY AAARVLQMAE HGEISLDNRV FVDADALVPN SPVTEARAGA
EMTLAELCQA ALQRSDNTAA NLLLKTIGGP AAVTAFARSV GDERTRLDRW EVELNSAIPG
DPRDTSTAAA LAVGYRAILA GDALSPPQRG LLEDWMRANQ TSSMRAGLPE GWTTADKTGS
GDYGSTNDAG IAFGPDGQRL LLVMMTRSQA HDPKAENLRP LIGELTALVL PSLL
//
