ID P94458_BACLI Unreviewed; 265 AA.
AC P94458;
DT 01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE Flags: Fragment;
GN Name=bla {ECO:0000313|EMBL:CAA71115.1};
OS Bacillus licheniformis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402 {ECO:0000313|EMBL:CAA71115.1};
RN [1] {ECO:0000313|EMBL:CAA71115.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BS3 {ECO:0000313|EMBL:CAA71115.1};
RA Duez C.M.J.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAA71115.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BS3 {ECO:0000313|EMBL:CAA71115.1};
RX PubMed=9280280; DOI=10.1016/S0014-5793(97)00908-3;
RA Ledent P., Duez C., Vanhove M., Lejeune A., Fonze E., Charlier P.,
RA Rhazi-Filali F., Thamm I., Guillaume G., Samyn B., Devreese B.,
RA Van Beeumen J., Lamotte-Brasseur J., Frere J.M.;
RT "Unexpected influence of a C-terminal-fused His-tag on the processing of an
RT enzyme and on the kinetic and folding parameters.";
RL FEBS Lett. 413:194-196(1997).
RN [3] {ECO:0007829|PDB:2X71}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
RX PubMed=20593835; DOI=10.1021/jm100437u;
RA Brown T., Charlier P., Herman R., Schofield C.J., Sauvage E.;
RT "Structural basis for the interaction of lactivicins with serine beta-
RT lactamases.";
RL J. Med. Chem. 53:5890-5894(2010).
RN [4] {ECO:0007829|PDB:4A5R}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
RA Power P., Herman R., Kerff F., Mercuri P., Galleni M., Gutkind G.,
RA Charlier P., Sauvage E.;
RT "Crystal Structure of Class a Beta-Lactamase from Bacillus Licheniformis
RT Inhibited by Tazobactam.";
RL Submitted (OCT-2011) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001526,
CC ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; Y10006; CAA71115.1; -; Genomic_DNA.
DR PDB; 2X71; X-ray; 2.10 A; A/B=1-265.
DR PDB; 4A5R; X-ray; 2.10 A; A/B=1-265.
DR PDBsum; 2X71; -.
DR PDBsum; 4A5R; -.
DR AlphaFoldDB; P94458; -.
DR SMR; P94458; -.
DR BRENDA; 3.5.2.6; 669.
DR EvolutionaryTrace; P94458; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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 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.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2X71, ECO:0007829|PDB:4A5R};
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 20..234
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAA71115.1"
FT NON_TER 265
FT /evidence="ECO:0000313|EMBL:CAA71115.1"
SQ SEQUENCE 265 AA; 29474 MW; BEA3E9418DCDA345 CRC64;
KTEMKDDFAK LEEQFDAKLG IFALDTGTNR TVTYRPDERF AFASTIKALT VGVLLQQKSI
EDLNQRITYT RDDLVNYNPI TEKHVDTGMT LKELADASLR YSDNTAQNLI LKQIGGPESL
KKELRKIGDE VTNPERFEPE LNEVNPGETQ DTSTARALAT SLQAFALEDK LPSEKRELLI
DWMKRNTTGD ALIRAGVPEG WEVADKTGAG SYGTRNDIAI IWPPKGDPVV LAVLSSRDKK
DAKYDDKLIA EATKVVVKAL NMNGK
//
