ID G7UQ38_PSEUP Unreviewed; 474 AA.
AC G7UQ38;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN OrderedLocusNames=DSC_11390 {ECO:0000313|EMBL:AER56922.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER56922.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER56922.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER56922.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU365093}; Single-pass membrane protein
CC {ECO:0000256|RuleBase:RU365093}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477, ECO:0000256|RuleBase:RU365093}.
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DR EMBL; CP003093; AER56922.1; -; Genomic_DNA.
DR RefSeq; WP_014161095.1; NC_016147.2.
DR AlphaFoldDB; G7UQ38; -.
DR STRING; 1045855.DSC_11390; -.
DR KEGG; psd:DSC_11390; -.
DR eggNOG; COG0845; Bacteria.
DR HOGENOM; CLU_023976_0_1_6; -.
DR OrthoDB; 9775513at2; -.
DR Proteomes; UP000005870; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR006144; Secretion_HlyD_CS.
DR InterPro; IPR010129; T1SS_HlyD.
DR NCBIfam; TIGR01843; type_I_hlyD; 1.
DR PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR PANTHER; PTHR30386:SF26; TRANSPORT PROTEIN COMB; 1.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF13437; HlyD_3; 1.
DR PRINTS; PR01490; RTXTOXIND.
DR PROSITE; PS00543; HLYD_FAMILY; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|RuleBase:RU365093};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU365093}; Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365093};
KW Reference proteome {ECO:0000313|Proteomes:UP000005870};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 105..131
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 191..218
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 474 AA; 52499 MW; 6A0E462441680CAC CRC64;
MKHVWEGAKE FLGRYRQAFG AAWKIRDLLD PPKRTEDELA FLPAQLELVE SPTSPAARWT
ARIIMALFCV ALLWAIVGKL DIVAVAPGKT VVGSRTKVIQ TAETAVVRSI RVKDGQTVRR
GDLLIELDAT ATGADYRQAD DALDSARLAE LRHAAMTQAL GTDRLPAPPL PIPGIAEDRL
QSAWQLTGSE FASFQAQQQR LKATIEQQQA QAQTVRSQID PLQRSLSIAR ERVADMERLL
GSQYVSKHEY LARKQEMVEM ERLLAAQQAT LVESQSAIAG AREELRVLIA DTRQKTYDGL
RQAREQIGQY APQVAKTEQR DKLMQLRAPV EGTVQQLAIH TVGGVVTPAQ ALMAIVPSEE
LLEVEATVLN KDIGFVRPGQ RATVKVESFP YTRYGYLEGI VETVSHDAAQ DENLGLIFPA
RVKLQNASLV IDGVKVMLTP GMSLSVEIKT GKRRVIDYLL SPLQEHTTEA FKER
//
