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 02-SEP-2026, entry version 106. DE RecName: Full=Beta-lactamase; DE EC=3.5.2.6; DE AltName: Full=Penicillinase; DE Flags: Precursor; OS Streptomyces albus G. OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; 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 AMINO ACID NUMBERING SCHEME. RX PubMed=2039479; DOI=10.1042/bj2760269; RA Ambler R.P., Coulson A.F., Frere J.M., Ghuysen J.M., Joris B., Forsman M., RA Levesque R.C., Tiraby G., Waley S.G.; RT "A standard numbering scheme for the class A beta-lactamases."; RL Biochem. J. 276:269-270(1991). RN [4] 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 -!- MISCELLANEOUS: The class A beta-lactamase family has a specific amino- CC acid numbering system, sometimes called Ambler or ABL numbering and CC often misspelt as Amber. A multiple sequence alignment was used to CC derive a consensus sequence and then the consensus was numbered taking CC into account insertions and deletions. This allows use of identical CC numbers, e.g. for active site residues, despite differences in protein CC length. UniProt always uses natural numbering of residues, hence there CC appear to be differences in numbering between this entry and some CC papers. {ECO:0000305|PubMed:2039479}. 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; M28303; AAA26775.1; -; Genomic_DNA. DR PIR; S00057; PNSM1U. DR PDB; 1BSG; X-ray; 1.85 A; A=47-314. DR AlphaFoldDB; P14559; -. DR MDposit; P14559; -. DR SMR; P14559; -. DR CARD; ARO:3003564; EXO-1; ARO:0001004; antibiotic inactivation. 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:InterPro. 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; IPR058160; BlaC_streptomyces. DR InterPro; IPR006311; TAT_signal. DR NCBIfam; NF033103; bla_class_A; 1. DR NCBIfam; NF033099; bla_Exo; 1. DR PANTHER; PTHR35333; BETA-LACTAMASE; 1. DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE-TYPE TRANSPEPTIDASE FOLD 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. DR PDBsum; 1BSG; -. 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..98 FT /evidence="ECO:0007829|PDB:1BSG" FT HELIX 99..103 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 295..297 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 //