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Database: UniProt
Entry: Q3KD93_PSEPF
LinkDB: Q3KD93_PSEPF
Original site: Q3KD93_PSEPF 
ID   Q3KD93_PSEPF            Unreviewed;       435 AA.
AC   Q3KD93;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   SubName: Full=Multidrug efflux system inner membrane protein {ECO:0000313|EMBL:ABA74262.1};
GN   OrderedLocusNames=Pfl01_2521 {ECO:0000313|EMBL:ABA74262.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA74262.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA74262.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA74262.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000256|ARBA:ARBA00009477}.
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DR   EMBL; CP000094; ABA74262.1; -; Genomic_DNA.
DR   RefSeq; WP_011333940.1; NC_007492.2.
DR   AlphaFoldDB; Q3KD93; -.
DR   KEGG; pfo:Pfl01_2521; -.
DR   eggNOG; COG0845; Bacteria.
DR   HOGENOM; CLU_018816_2_0_6; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 2.40.30.170; -; 1.
DR   Gene3D; 2.40.420.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR   InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR   InterPro; IPR006143; RND_pump_MFP.
DR   NCBIfam; TIGR01730; RND_mfp; 1.
DR   PANTHER; PTHR30469; MULTIDRUG RESISTANCE PROTEIN MDTA; 1.
DR   PANTHER; PTHR30469:SF12; MULTIDRUG RESISTANCE PROTEIN MDTA; 1.
DR   Pfam; PF13533; Biotin_lipoyl_2; 1.
DR   Pfam; PF13437; HlyD_3; 1.
DR   SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT   DOMAIN          96..143
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   REGION          394..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   435 AA;  46604 MW;  A89A7D30C334F210 CRC64;
     MVNQSMQSSS RNSRRWLLSL LVLLVIAGLC WKFWPSGSTH KEGGEKAQAG HTGRSGMMRP
     GFGGAAGPIP VRVAPAVTGD FPLYYKALGT VTALNTINVR SRVGGELVKI YFEEGQMVKA
     GDLLAEIDPR PYQNALLQAE GTLLQNQAQL KNAQVDVERY RGLYKEDSIA KQTLDTAEAL
     VGQYLGTVKT NQAAVNDAKL NLEFTKIRAP IAGRVGLRQL DVGNLVAAND TTSLAVITQT
     QPISVAFTLP ENSLDTVLAR YRSGAKLPAE AWDRGDTKLQ ATGVLQSLDN QIDVTTGTLK
     FKARYENRDQ SLFPNQFVNV HLLADTLKGV VLAPSAAIQF GTNGTFVYAL DGDKKVTIRQ
     LKIGASDGEN TVVTEGLAAG DRVVLEGTDR LKEGSEVEVV NDSKDVPTTP TEHLQGKSAA
     TAPDAAVTDK AKKGA
//
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