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Beta-lactamase AST-1 (EC 3.5.2.6)

 BLAC_NOCAS              Reviewed;         310 AA.
Q9EZQ7;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 62.
RecName: Full=Beta-lactamase AST-1;
EC=3.5.2.6;
Flags: Precursor;
Name=bla; Synonyms=ast1;
Nocardia asteroides.
Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
NCBI_TaxID=1824;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ACTIVITY REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11181374; DOI=10.1128/AAC.45.3.878-882.2001;
Poirel L., Laurent F., Naas T., Labia R., Boiron P., Nordmann P.;
"Molecular and biochemical analysis of AST-1, a class A beta-lactamase
from Nocardia asteroides sensu stricto.";
Antimicrob. Agents Chemother. 45:878-882(2001).
-!- FUNCTION: Confers high levels of resistance to amoxicillin,
benzylpenicillin, piperacillin, ticarcillin and cephalothin. Not
active against ceftazidime, cefotaxime and aztreonam.
-!- CATALYTIC ACTIVITY:
Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE-
ProRule:PRU10101};
-!- ACTIVITY REGULATION: Inhibited by clavulanic acid.
{ECO:0000269|PubMed:11181374}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=30 uM for benzylpenicillin {ECO:0000269|PubMed:11181374};
KM=50 uM for amoxicillin {ECO:0000269|PubMed:11181374};
KM=7 uM for ticarcillin {ECO:0000269|PubMed:11181374};
KM=330 uM for piperacillin {ECO:0000269|PubMed:11181374};
KM=20 uM for cephalothin {ECO:0000269|PubMed:11181374};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}.
-!- SIMILARITY: Belongs to the class-A beta-lactamase family.
{ECO:0000305}.
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EMBL; AF279904; AAG44836.1; -; Genomic_DNA.
RefSeq; WP_063857821.1; NG_048690.1.
ProteinModelPortal; Q9EZQ7; -.
SMR; Q9EZQ7; -.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR000871; Beta-lactam_class-A.
InterPro; IPR023650; Beta-lactam_class-A_AS.
PRINTS; PR00118; BLACTAMASEA.
SUPFAM; SSF56601; SSF56601; 1.
PROSITE; PS00146; BETA_LACTAMASE_A; 1.
1: Evidence at protein level;
Antibiotic resistance; Cell membrane; Hydrolase; Lipoprotein;
Membrane; Palmitate; Signal.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 310 Beta-lactamase AST-1.
/FTId=PRO_0000313797.
REGION 255 257 Substrate binding. {ECO:0000250}.
ACT_SITE 91 91 Acyl-ester intermediate.
{ECO:0000250|UniProtKB:P9WKD3}.
ACT_SITE 187 187 Proton acceptor.
{ECO:0000250|UniProtKB:P9WKD3}.
BINDING 151 151 Substrate.
{ECO:0000250|UniProtKB:P9WKD3}.
SITE 94 94 Increases nucleophilicity of active site
Ser. {ECO:0000250|UniProtKB:P9WKD3}.
LIPID 32 32 N-palmitoyl cysteine. {ECO:0000255}.
LIPID 32 32 S-diacylglycerol cysteine. {ECO:0000255}.
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


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