BLAC_NOCFA
ID BLAC_NOCFA Reviewed; 313 AA.
AC Q5YXD6; O30987;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Beta-lactamase FAR-1;
DE EC=3.5.2.6;
DE Flags: Precursor;
GN Name=bla; Synonyms=far1; OrderedLocusNames=NFA_23080;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=VIC;
RX PubMed=10390216; DOI=10.1128/aac.43.7.1644;
RA Laurent F., Poirel L., Naas T., Chaibi E.B., Labia R., Boiron P.,
RA Nordmann P.;
RT "Biochemical-genetic analysis and distribution of FAR-1, a class A beta-
RT lactamase from Nocardia farcinica.";
RL Antimicrob. Agents Chemother. 43:1644-1650(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
RN [3]
RP EVIDENCE OF MEMBRANE-BOUND LOCALIZATION.
RX PubMed=8239595; DOI=10.1128/aac.37.9.1850;
RA Steingrube V.A., Wallace R.J., Brown B.A., Zhang Y., Steele L.C., Young G.,
RA Nash D.R.;
RT "Partial characterization of Nocardia farcinica beta-lactamases.";
RL Antimicrob. Agents Chemother. 37:1850-1855(1993).
CC -!- FUNCTION: Confers high levels of resistance to amoxicillin,
CC benzylpenicillin, piperacillin, ticarcillin and cephalothin. Also
CC hydrolyzes aztreonam at a low level. Not active against ceftazidime,
CC cefotaxime and imipenem.
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, and at a low level
CC by tazobactam and sulbactam. {ECO:0000269|PubMed:10390216}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for benzylpenicillin {ECO:0000269|PubMed:10390216};
CC KM=50 uM for amoxicillin {ECO:0000269|PubMed:10390216};
CC KM=31 uM for ticarcillin {ECO:0000269|PubMed:10390216};
CC KM=45 uM for piperacillin {ECO:0000269|PubMed:10390216};
CC KM=104 uM for cephalothin {ECO:0000269|PubMed:10390216};
CC KM=400 uM for aztreonam {ECO:0000269|PubMed:10390216};
CC Vmax=5.5 umol/sec/mg enzyme with benzylpenicillin as substrate
CC {ECO:0000269|PubMed:10390216};
CC Vmax=3.8 umol/sec/mg enzyme with amoxicillin as substrate
CC {ECO:0000269|PubMed:10390216};
CC Vmax=1.6 umol/sec/mg enzyme with ticarcillin as substrate
CC {ECO:0000269|PubMed:10390216};
CC Vmax=9.2 umol/sec/mg enzyme with piperacillin as substrate
CC {ECO:0000269|PubMed:10390216};
CC Vmax=0.13 umol/sec/mg enzyme with cephalothin as substrate
CC {ECO:0000269|PubMed:10390216};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB81957.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD57155.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF024601; AAB81957.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AP006618; BAD57155.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5YXD6; -.
DR SMR; Q5YXD6; -.
DR EnsemblBacteria; BAD57155; BAD57155; NFA_23080.
DR KEGG; nfa:NFA_23080; -.
DR eggNOG; COG2367; Bacteria.
DR HOGENOM; CLU_031960_6_0_11; -.
DR OMA; FKTLACA; -.
DR SABIO-RK; Q5YXD6; -.
DR Proteomes; UP000006820; Chromosome.
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; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..313
FT /note="Beta-lactamase FAR-1"
FT /id="PRO_0000313798"
FT ACT_SITE 94
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT BINDING 258..260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 97
FT /note="Increases nucleophilicity of active site Ser"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT LIPID 29
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 29
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
FT CONFLICT 22
FT /note="V -> A (in Ref. 1; AAB81957)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="A -> T (in Ref. 1; AAB81957)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="F -> S (in Ref. 1; AAB81957)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="V -> E (in Ref. 1; AAB81957)"
FT /evidence="ECO:0000305"
SQ 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
