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Beta-lactamase FAR-1 (EC 3.5.2.6)

 BLAC_NOCFA              Reviewed;         313 AA.
Q5YXD6; O30987;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 2.
07-JUN-2017, entry version 82.
RecName: Full=Beta-lactamase FAR-1;
EC=3.5.2.6;
Flags: Precursor;
Name=bla; Synonyms=far1; OrderedLocusNames=NFA_23080;
Nocardia farcinica (strain IFM 10152).
Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
NCBI_TaxID=247156;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=VIC;
PubMed=10390216;
Laurent F., Poirel L., Naas T., Chaibi E.B., Labia R., Boiron P.,
Nordmann P.;
"Biochemical-genetic analysis and distribution of FAR-1, a class A
beta-lactamase from Nocardia farcinica.";
Antimicrob. Agents Chemother. 43:1644-1650(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IFM 10152;
PubMed=15466710; DOI=10.1073/pnas.0406410101;
Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
Shiba T., Hattori M.;
"The complete genomic sequence of Nocardia farcinica IFM 10152.";
Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
[3]
EVIDENCE OF MEMBRANE-BOUND LOCALIZATION.
PubMed=8239595; DOI=10.1128/AAC.37.9.1850;
Steingrube V.A., Wallace R.J., Brown B.A., Zhang Y., Steele L.C.,
Young G., Nash D.R.;
"Partial characterization of Nocardia farcinica beta-lactamases.";
Antimicrob. Agents Chemother. 37:1850-1855(1993).
-!- FUNCTION: Confers high levels of resistance to amoxicillin,
benzylpenicillin, piperacillin, ticarcillin and cephalothin. Also
hydrolyzes aztreonam at a low level. Not active against
ceftazidime, cefotaxime and imipenem.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000255|PROSITE-ProRule:PRU10101}.
-!- ENZYME REGULATION: Inhibited by clavulanic acid, and at a low
level by tazobactam and sulbactam. {ECO:0000269|PubMed:10390216}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=30 uM for benzylpenicillin {ECO:0000269|PubMed:10390216};
KM=50 uM for amoxicillin {ECO:0000269|PubMed:10390216};
KM=31 uM for ticarcillin {ECO:0000269|PubMed:10390216};
KM=45 uM for piperacillin {ECO:0000269|PubMed:10390216};
KM=104 uM for cephalothin {ECO:0000269|PubMed:10390216};
KM=400 uM for aztreonam {ECO:0000269|PubMed:10390216};
Vmax=5.5 umol/sec/mg enzyme with benzylpenicillin as substrate
{ECO:0000269|PubMed:10390216};
Vmax=3.8 umol/sec/mg enzyme with amoxicillin as substrate
{ECO:0000269|PubMed:10390216};
Vmax=1.6 umol/sec/mg enzyme with ticarcillin as substrate
{ECO:0000269|PubMed:10390216};
Vmax=9.2 umol/sec/mg enzyme with piperacillin as substrate
{ECO:0000269|PubMed:10390216};
Vmax=0.13 umol/sec/mg enzyme with cephalothin as substrate
{ECO:0000269|PubMed:10390216};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}.
-!- SIMILARITY: Belongs to the class-A beta-lactamase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB81957.1; Type=Frameshift; Positions=2; Evidence={ECO:0000305};
Sequence=BAD57155.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF024601; AAB81957.1; ALT_FRAME; Genomic_DNA.
EMBL; AP006618; BAD57155.1; ALT_INIT; Genomic_DNA.
ProteinModelPortal; Q5YXD6; -.
SMR; Q5YXD6; -.
STRING; 247156.nfa23080; -.
EnsemblBacteria; BAD57155; BAD57155; NFA_23080.
KEGG; nfa:NFA_23080; -.
eggNOG; ENOG4108J4B; Bacteria.
eggNOG; COG2367; LUCA.
KO; K17836; -.
OMA; FKTLACA; -.
OrthoDB; POG091H023N; -.
SABIO-RK; Q5YXD6; -.
Proteomes; UP000006820; Chromosome.
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; Complete proteome; Hydrolase;
Lipoprotein; Membrane; Palmitate; Reference proteome; Signal.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 313 Beta-lactamase FAR-1.
/FTId=PRO_0000313798.
REGION 258 260 Substrate binding. {ECO:0000250}.
ACT_SITE 94 94 Acyl-ester intermediate.
{ECO:0000250|UniProtKB:P9WKD3}.
ACT_SITE 190 190 Proton acceptor.
{ECO:0000250|UniProtKB:P9WKD3}.
BINDING 154 154 Substrate.
{ECO:0000250|UniProtKB:P9WKD3}.
SITE 97 97 Increases nucleophilicity of active site
Ser. {ECO:0000250|UniProtKB:P9WKD3}.
LIPID 29 29 N-palmitoyl cysteine. {ECO:0000255}.
LIPID 29 29 S-diacylglycerol cysteine. {ECO:0000255}.
CONFLICT 22 22 V -> A (in Ref. 1; AAB81957).
{ECO:0000305}.
CONFLICT 49 49 A -> T (in Ref. 1; AAB81957).
{ECO:0000305}.
CONFLICT 65 65 F -> S (in Ref. 1; AAB81957).
{ECO:0000305}.
CONFLICT 81 81 V -> E (in Ref. 1; AAB81957).
{ECO:0000305}.
SEQUENCE 313 AA; 32566 MW; EB60AB1DC46B841D CRC64;
MPGVDISFLK KSGRRTMAAA AVIALLGGCG ADAGSEPATT AASTTAPSAA TDAATAEFAA
LEQRFGARLG VYAVDTTSGA VVAYRADERF GMASTFKGLA CGALLREHPL SSGYFDQVVR
YSREEVVSYS PVTETRVDTG MTVAELCHAT ITVSDNTAGN QILKLLGGPA GFTAFLRSLG
DEVSRLDRWE TELNEVPPGE ERDTTTPAAV AANYRALVLG DVLAEPERAQ LRDWLVANTT
GDQRIRAGVP AGWTVGDKTG GGSHGGNNDV AVAWTETGDP IVIALLSHRT DPAAKADNAL
LAEATRAVVT ALR


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