ID FUSA_BURCE Reviewed; 530 AA. AC P24126; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 14-DEC-2022, entry version 89. DE RecName: Full=Fusaric acid resistance protein FusA; DE Flags: Precursor; GN Name=fusA; OS Burkholderia cepacia (Pseudomonas cepacia). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=UK1; RX PubMed=1370369; DOI=10.1271/bbb1961.55.1913; RA Utsumi R., Yagi T., Katayama S., Katsuragi K., Tachibana K., Toyoda H., RA Ouchi S., Obata K., Shibano Y., Noda M.; RT "Molecular cloning and characterization of the fusaric acid-resistance gene RT from Pseudomonas cepacia."; RL Agric. Biol. Chem. 55:1913-1918(1991). RN [2] RP CONCEPTUAL TRANSLATION. RA Rudd K.E.; RL Unpublished observations (JUN-1999). CC -!- FUNCTION: Involved in the resistance (detoxification) of the fungal CC toxin fusaric acid. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC60388.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA02064.1; Type=Frameshift; Evidence={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; S77489; AAC60388.1; ALT_FRAME; Genomic_DNA. DR EMBL; D12503; BAA02064.1; ALT_FRAME; Genomic_DNA. DR PIR; JU0396; JU0396. DR TCDB; 1.B.17.3.2; the outer membrane factor (omf) family. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003423; OMP_efflux. DR InterPro; IPR010131; RND_efflux_OM_lipoprot_NodT. DR Pfam; PF02321; OEP; 2. DR TIGRFAMs; TIGR01845; outer_NodT; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Lipoprotein; Membrane; Palmitate; Signal; Transmembrane; KW Transmembrane beta strand. FT SIGNAL 1..23 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT CHAIN 24..530 FT /note="Fusaric acid resistance protein FusA" FT /id="PRO_0000030995" FT REGION 378..442 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 475..530 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 384..417 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 24 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT LIPID 24 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" SQ SEQUENCE 530 AA; 55848 MW; 434755D9395F0EE4 CRC64; MQSPATKGTL ALAVLAVSLI MAGCASMGDN KPQSARIEAN ALDAGAAIRA ADRDAGWPAA DWWRAYRDPQ LDTWIAAAQA GXPDARGRRG RVREAQAMAR VARSAELPQI NGNLSLMRQH WPDNVYYGPG PLANTDTWNN TGTLGLSYHL DLWGKDKNAT ERALDTAHAT AADARAAKLE LEVNVVRAYV GMSMNYALLD LAHETFERQR SLADLARKRL QAGLGTQLEV SQAESTLPDY ERQIDSYEEA IQLARHQLAA LAGKGPGAGD AIKRPRLSLD APAGLPSAMP ADLLGRRPDV VAARWTVDAQ ARGIDVAKAS FYPNIDLLAT VGGFGVTAPF TDFLRAMNGG WTAGPALSLP IFEGGRLRAQ LGAANAGVRP GGRAIQPDDR RRAQGHRRPG RADPFARYAE EGRRTLGGRQ RPQLPAVARR LPPRPDRLRQ RAGRAAAIVG AHRKRPPHRS ERLAAHAQLM AALGGGVETG TDVPGSQSSH GESAAGAAAP AAASGAKPVA AAARPAQVAA AGAAGVPAAR //