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FUSA_BURCE
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   02-JUN-2021, entry version 87.
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RL   Unpublished observations (JUN-1999).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};
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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   PRIDE; P24126; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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
 
 
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