ID   BLAC_NOCAS              Reviewed;         310 AA.
AC   Q9EZQ7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Beta-lactamase AST-1;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=ast1;
OS   Nocardia asteroides.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=1824;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11181374; DOI=10.1128/aac.45.3.878-882.2001;
RA   Poirel L., Laurent F., Naas T., Labia R., Boiron P., Nordmann P.;
RT   "Molecular and biochemical analysis of AST-1, a class A beta-lactamase from
RT   Nocardia asteroides sensu stricto.";
RL   Antimicrob. Agents Chemother. 45:878-882(2001).
CC   -!- FUNCTION: Confers high levels of resistance to amoxicillin,
CC       benzylpenicillin, piperacillin, ticarcillin and cephalothin. Not active
CC       against ceftazidime, cefotaxime and aztreonam.
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   -!- ACTIVITY REGULATION: Inhibited by clavulanic acid.
CC       {ECO:0000269|PubMed:11181374}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=30 uM for benzylpenicillin {ECO:0000269|PubMed:11181374};
CC         KM=50 uM for amoxicillin {ECO:0000269|PubMed:11181374};
CC         KM=7 uM for ticarcillin {ECO:0000269|PubMed:11181374};
CC         KM=330 uM for piperacillin {ECO:0000269|PubMed:11181374};
CC         KM=20 uM for cephalothin {ECO:0000269|PubMed:11181374};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; AF279904; AAG44836.1; -; Genomic_DNA.
DR   RefSeq; WP_063857821.1; NG_048690.1.
DR   AlphaFoldDB; Q9EZQ7; -.
DR   SMR; Q9EZQ7; -.
DR   SABIO-RK; Q9EZQ7; -.
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.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Cell membrane; Hydrolase; Lipoprotein; Membrane;
KW   Palmitate; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..310
FT                   /note="Beta-lactamase AST-1"
FT                   /id="PRO_0000313797"
FT   ACT_SITE        91
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT   BINDING         255..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            94
FT                   /note="Increases nucleophilicity of active site Ser"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT   LIPID           32
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           32
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   310 AA;  32476 MW;  53668F7DBFF1A6B3 CRC64;
     MTFSALPFRR ADRRRLLAAA LAACALTLTA ACDSGTVTVP VTDSVTTSAV ADPRFAELET
     TSGARLGVFA VDTGSGRTVA HRADERFPMA STFKGLACGA LLREHPLSTG YFDQVIHYSA
     AELVEYSPVT ETRVETGMTV RELCDAAITV SDNTAGNQLL KLLGGPEGFT ASLRSLGDAT
     SRLDRWETDL NTAIPGDERD TTTPAALAAD YRALVVGDVL GAPERDQLKA WLVANTTGAT
     RIRAGLPADW TVGDKTGSPA YGSALDVAVA WPPGRAPIVI AVLSTKSEQD AEPDNALLAE
     ATRVVVDALG