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Database: UniProt
Entry: E1SHS0_PANVC
LinkDB: E1SHS0_PANVC
Original site: E1SHS0_PANVC 
ID   E1SHS0_PANVC            Unreviewed;       384 AA.
AC   E1SHS0;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Multidrug resistance protein A {ECO:0000313|EMBL:ADO08869.1};
GN   Name=emra1 {ECO:0000313|EMBL:ADO08869.1};
GN   OrderedLocusNames=Pvag_0667 {ECO:0000313|EMBL:ADO08869.1};
OS   Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO08869.1, ECO:0000313|Proteomes:UP000006631};
RN   [1] {ECO:0000313|EMBL:ADO08869.1, ECO:0000313|Proteomes:UP000006631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C9-1 {ECO:0000313|EMBL:ADO08869.1,
RC   ECO:0000313|Proteomes:UP000006631};
RX   PubMed=20952567; DOI=10.1128/JB.01122-10;
RA   Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA   Stockwell V.O., Frey J.E., Duffy B.;
RT   "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL   J. Bacteriol. 192:6486-6487(2010).
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; CP002206; ADO08869.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1SHS0; -.
DR   KEGG; pva:Pvag_0667; -.
DR   eggNOG; COG1566; Bacteria.
DR   HOGENOM; CLU_018816_15_1_6; -.
DR   Proteomes; UP000006631; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.170; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 1.10.287.470; Helix hairpin bin; 2.
DR   InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR   PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR   PANTHER; PTHR30386:SF19; MULTIDRUG EXPORT PROTEIN EMRA-RELATED; 1.
DR   Pfam; PF13533; Biotin_lipoyl_2; 1.
DR   Pfam; PF13437; HlyD_3; 1.
DR   SUPFAM; SSF111369; HlyD-like secretion proteins; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        47..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          84..130
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          123..250
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        11..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  42461 MW;  462297A902EDA0FF CRC64;
     MGTMSENNQR DQHQQDADNA TDKSRQSEEN QDNDQQPERK RPGKKPLIIL AVVVVVMLIV
     GFWFWFSTRN IETTDDAFTE GDAVTIAPKA SGYVVKLLVK DNQRVKKGDL LVEIDPSDNR
     AQREQANAQL GLAVAQLHQA QAQLALSKVQ YPAQRDQALA DQAKAEANLL NAQADYRRQR
     GVDPRATSQR NIDSASAQLR SAQAQLQSAK AQVEVASQVA LQIRQQETNV EARQQQVEQA
     KAQLSTADLN LSYTQVRAPY DGFITKRNVQ LGTLVQAGSS LFSLVSPEIW VTANFKESQL
     QRMNPGDKVE ISVDAWPDMK LEGHVDSIQM GSGSRFSTFP SENATGNYVK IVQRVPVKIV
     IDKGLDPNHP LPLGLSVEPK VTVE
//
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