BLAC_STRAL
ID BLAC_STRAL Reviewed; 314 AA.
AC P14559;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Beta-lactamase;
DE EC=3.5.2.6;
DE AltName: Full=Penicillinase;
DE Flags: Precursor;
OS Streptomyces albus G.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3038538; DOI=10.1111/j.1432-1033.1987.tb13521.x;
RA Dehottay P., Dusart J., de Meester F., Joris B., van Beeumen J.,
RA Erpicum T., Frere J.-M., Ghuysen J.-M.;
RT "Nucleotide sequence of the gene encoding the Streptomyces albus G beta-
RT lactamase precursor.";
RL Eur. J. Biochem. 166:345-350(1987).
RN [2]
RP PROTEIN SEQUENCE OF 81-92, AND ACTIVE SITE SER-89.
RX PubMed=2822004; DOI=10.1042/bj2440427;
RA de Meester F., Joris B., Lenzini M.V., Dehottay P., Erpicium T., Dusart J.,
RA Klein D., Ghuysen J.-M., Frere J.-M., van Beeumen J.;
RT "The active sites of the beta-lactamases of Streptomyces cacaoi and
RT Streptomyces albus G.";
RL Biochem. J. 244:427-432(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 47-314.
RA Fonze E., Charlier P., Dideberg O.;
RL Submitted (JUL-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; M28303; AAA26775.1; -; Genomic_DNA.
DR PIR; S00057; PNSM1U.
DR PDB; 1BSG; X-ray; 1.85 A; A=47-314.
DR PDBsum; 1BSG; -.
DR AlphaFoldDB; P14559; -.
DR SMR; P14559; -.
DR EvolutionaryTrace; P14559; -.
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 InterPro; IPR006311; TAT_signal.
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; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase;
KW Signal.
FT SIGNAL 1..39
FT /note="Tat-type signal"
FT CHAIN 40..314
FT /note="Beta-lactamase"
FT /id="PRO_0000017012"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 89
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10101,
FT ECO:0000269|PubMed:2822004"
FT BINDING 259..261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:1BSG"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:1BSG"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1BSG"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:1BSG"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1BSG"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:1BSG"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:1BSG"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 226..237
FT /evidence="ECO:0007829|PDB:1BSG"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:1BSG"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:1BSG"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:1BSG"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:1BSG"
FT HELIX 299..312
FT /evidence="ECO:0007829|PDB:1BSG"
SQ SEQUENCE 314 AA; 33265 MW; 5A17D7D19C84E511 CRC64;
MHPSTSRPSR RTLLTATAGA ALAAATLVPG TAHASSGGRG HGSGSVSDAE RRLAGLERAS
GARLGVYAYD TGSGRTVAYR ADELFPMCSV FKTLSSAAVL RDLDRNGEFL SRRILYTQDD
VEQADGAGPE TGKPQNLANA QLTVEELCEV SITASDNCAA NLMLRELGGP AAVTRFVRSL
GDRVTRLDRW EPELNSAEPG RVTDTTSPRA ITRTYGRLVL GDALNPRDRR LLTSWLLANT
TSGDRFRAGL PDDWTLGDKT GAGRYGTNND AGVTWPPGRA PIVLTVLTAK TEQDAARDDG
LVADAARVLA ETLG
