BLAC_BACLI
ID BLAC_BACLI Reviewed; 307 AA.
AC P00808;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Beta-lactamase;
DE EC=3.5.2.6;
DE AltName: Full=Penicillinase;
DE Contains:
DE RecName: Full=Large exopenicillinase;
DE Contains:
DE RecName: Full=Small exopenicillinase;
DE Flags: Precursor;
GN Name=penP; Synonyms=blaP;
OS Bacillus licheniformis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25972 / DSM 8782 / NCIMB 11109 / IMET 10723 / 749/C;
RX PubMed=6269055; DOI=10.1093/nar/9.11.2577;
RA Neugebauer K., Sprengel R., Schaller H.;
RT "Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene
RT and implications for the biosynthesis of a secretory protein in a Gram-
RT positive bacterium.";
RL Nucleic Acids Res. 9:2577-2588(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RC STRAIN=ATCC 25972 / DSM 8782 / NCIMB 11109 / IMET 10723 / 749/C;
RX PubMed=6977472; DOI=10.1016/0378-1119(81)90177-3;
RA Kroyer J., Chang S.;
RT "The promoter-proximal region of the Bacillus licheniformis penicillinase
RT gene: nucleotide sequence and predicted leader peptide sequence.";
RL Gene 15:343-347(1981).
RN [3]
RP PROTEIN SEQUENCE OF 43-307.
RX PubMed=5353499; DOI=10.1042/bj1150012pb;
RA Meadway R.J.;
RT "The amino acid sequence of penicillinase from Bacillus licheniformis.";
RL Biochem. J. 115:12P-13P(1969).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RC STRAIN=ATCC 25972 / DSM 8782 / NCIMB 11109 / IMET 10723 / 749/C;
RX PubMed=3260234; DOI=10.1128/jb.170.7.3206-3212.1988;
RA Wittman V., Wong H.C.;
RT "Regulation of the penicillinase genes of Bacillus licheniformis:
RT interaction of the pen repressor with its operators.";
RL J. Bacteriol. 170:3206-3212(1988).
RN [5]
RP CONFIRMATION OF THE AMINO ENDS OF THE LARGE AND SMALL EXOPENICILLINASE.
RX PubMed=6966510; DOI=10.1021/bi00550a023;
RA Izui K., Nielsen J.B.K., Caulfield M.P., Lampen J.O.;
RT "Large exopenicillinase, initial extracellular form detected in cultures of
RT Bacillus licheniformis.";
RL Biochemistry 19:1882-1886(1980).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2326252; DOI=10.1002/prot.340070205;
RA Moews P.C., Knox J.R., Dideberg O., Charlier P., Frere J.-M.;
RT "Beta-lactamase of Bacillus licheniformis 749/C at 2-A resolution.";
RL Proteins 7:156-171(1990).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1856867; DOI=10.1016/0022-2836(91)90023-y;
RA Knox J.R., Moews P.C.;
RT "Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2-A
RT resolution and analysis of hydration.";
RL J. Mol. Biol. 220:435-455(1991).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=11827533; DOI=10.1021/bi015789k;
RA Fonze E., Vanhove M., Dive G., Sauvage E., Frere J.-M., Charlier P.;
RT "Crystal structures of the Bacillus licheniformis BS3 class A beta-
RT lactamase and of the acyl-enzyme adduct formed with cefoxitin.";
RL Biochemistry 41:1877-1885(2002).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: By the bacillus licheniformis protein BlaR1.
CC -!- PTM: Large exopenicillinase is the primary secretion product; it can be
CC converted to small exopenicillinase.
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; V00093; CAA23431.1; -; Genomic_DNA.
DR EMBL; M21337; AAA22649.2; -; Genomic_DNA.
DR PIR; A93727; PNBSL.
DR RefSeq; WP_023857755.1; NG_051161.1.
DR PDB; 1I2S; X-ray; 1.70 A; A/B=26-307.
DR PDB; 1I2W; X-ray; 1.70 A; A/B=26-307.
DR PDB; 1MBL; X-ray; 2.00 A; A/B=48-303.
DR PDB; 1W7F; X-ray; 1.80 A; A/B=1-307.
DR PDB; 2BLM; X-ray; 2.00 A; A/B=43-307.
DR PDB; 2WK0; X-ray; 1.65 A; A/B=43-307.
DR PDB; 2Y91; X-ray; 2.00 A; A/B=43-307.
DR PDB; 3B3X; X-ray; 2.50 A; A/B=43-307.
DR PDB; 3LY3; X-ray; 1.80 A; A=47-305.
DR PDB; 3LY4; X-ray; 1.80 A; A=47-303.
DR PDB; 3M2J; X-ray; 1.80 A; A/B=47-303.
DR PDB; 3M2K; X-ray; 3.50 A; A/B=47-303.
DR PDB; 3SH7; X-ray; 2.50 A; A/B=43-307.
DR PDB; 3SH8; X-ray; 2.00 A; A/B=43-307.
DR PDB; 3SH9; X-ray; 1.90 A; A/B=43-307.
DR PDB; 3SOI; X-ray; 1.73 A; A/B=46-303.
DR PDB; 4BLM; X-ray; 2.00 A; A/B=43-307.
DR PDB; 4M3K; X-ray; 1.48 A; A=44-307.
DR PDB; 4N1H; X-ray; 3.00 A; A/C=44-307.
DR PDB; 4N92; X-ray; 1.93 A; A/B=43-307.
DR PDB; 4N9K; X-ray; 1.93 A; A/B=43-307.
DR PDB; 4N9L; X-ray; 2.30 A; A/B=43-307.
DR PDB; 5GHX; X-ray; 1.24 A; A/B=43-307.
DR PDB; 5GHY; X-ray; 2.10 A; A/B=43-307.
DR PDB; 5GHZ; X-ray; 1.93 A; A/B=43-307.
DR PDB; 5LWF; X-ray; 2.56 A; A/B=44-307.
DR PDB; 5ZFL; X-ray; 1.50 A; A/B=43-307.
DR PDB; 5ZFT; X-ray; 1.93 A; A/B=43-307.
DR PDB; 5ZG6; X-ray; 2.00 A; A/B=43-307.
DR PDBsum; 1I2S; -.
DR PDBsum; 1I2W; -.
DR PDBsum; 1MBL; -.
DR PDBsum; 1W7F; -.
DR PDBsum; 2BLM; -.
DR PDBsum; 2WK0; -.
DR PDBsum; 2Y91; -.
DR PDBsum; 3B3X; -.
DR PDBsum; 3LY3; -.
DR PDBsum; 3LY4; -.
DR PDBsum; 3M2J; -.
DR PDBsum; 3M2K; -.
DR PDBsum; 3SH7; -.
DR PDBsum; 3SH8; -.
DR PDBsum; 3SH9; -.
DR PDBsum; 3SOI; -.
DR PDBsum; 4BLM; -.
DR PDBsum; 4M3K; -.
DR PDBsum; 4N1H; -.
DR PDBsum; 4N92; -.
DR PDBsum; 4N9K; -.
DR PDBsum; 4N9L; -.
DR PDBsum; 5GHX; -.
DR PDBsum; 5GHY; -.
DR PDBsum; 5GHZ; -.
DR PDBsum; 5LWF; -.
DR PDBsum; 5ZFL; -.
DR PDBsum; 5ZFT; -.
DR PDBsum; 5ZG6; -.
DR AlphaFoldDB; P00808; -.
DR BMRB; P00808; -.
DR SMR; P00808; -.
DR BindingDB; P00808; -.
DR ChEMBL; CHEMBL5633; -.
DR DrugBank; DB04261; Carbamic Acid.
DR DrugBank; DB01331; Cefoxitin.
DR DrugBank; DB04272; Citric acid.
DR DrugCentral; P00808; -.
DR ABCD; P00808; 3 sequenced antibodies.
DR GeneID; 56670005; -.
DR BRENDA; 3.5.2.6; 669.
DR SABIO-RK; P00808; -.
DR EvolutionaryTrace; P00808; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell membrane;
KW Direct protein sequencing; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW Signal.
FT SIGNAL 1..26
FT CHAIN 27..307
FT /note="Large exopenicillinase"
FT /id="PRO_0000016973"
FT CHAIN 43..307
FT /note="Small exopenicillinase"
FT /id="PRO_0000016974"
FT ACT_SITE 86
FT /note="Acyl-ester intermediate"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT BINDING 248..250
FT /ligand="substrate"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:5GHX"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4M3K"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5GHX"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3SH8"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:5GHX"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:5GHX"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:5GHX"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:5GHX"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:5GHX"
SQ SEQUENCE 307 AA; 33996 MW; 7E25B1E72129A6DA CRC64;
MKLWFSTLKL KKAAAVLLFS CVALAGCANN QTNASQPAEK NEKTEMKDDF AKLEEQFDAK
LGIFALDTGT NRTVAYRPDE RFAFASTIKA LTVGVLLQQK SIEDLNQRIT YTRDDLVNYN
PITEKHVDTG MTLKELADAS LRYSDNAAQN LILKQIGGPE SLKKELRKIG DEVTNPERFE
PELNEVNPGE TQDTSTARAL VTSLRAFALE DKLPSEKREL LIDWMKRNTT GDALIRAGVP
DGWEVADKTG AASYGTRNDI AIIWPPKGDP VVLAVLSSRD KKDAKYDDKL IAEATKVVMK
ALNMNGK
