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Database: UniProt
Entry: A0A010RQP7_PSEFL
LinkDB: A0A010RQP7_PSEFL
Original site: A0A010RQP7_PSEFL 
ID   A0A010RQP7_PSEFL        Unreviewed;       391 AA.
AC   A0A010RQP7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=RND transporter MFP subunit {ECO:0000313|EMBL:EXF91334.1};
GN   ORFNames=HK44_018475 {ECO:0000313|EMBL:EXF91334.1};
OS   Pseudomonas fluorescens HK44.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF91334.1, ECO:0000313|Proteomes:UP000022611};
RN   [1] {ECO:0000313|EMBL:EXF91334.1, ECO:0000313|Proteomes:UP000022611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK44 {ECO:0000313|EMBL:EXF91334.1,
RC   ECO:0000313|Proteomes:UP000022611};
RX   PubMed=21742869; DOI=10.1128/JB.05530-11;
RA   Chauhan A., Layton A.C., Williams D.E., Smartt A.E., Ripp S.,
RA   Karpinets T.V., Brown S.D., Sayler G.S.;
RT   "Draft genome sequence of the polycyclic aromatic hydrocarbon-degrading,
RT   genetically engineered bioluminescent bioreporter Pseudomonas fluorescens
RT   HK44.";
RL   J. Bacteriol. 193:5009-5010(2011).
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000256|ARBA:ARBA00009477}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXF91334.1}.
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DR   EMBL; AFOY02000026; EXF91334.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A010RQP7; -.
DR   PATRIC; fig|1042209.11.peg.5862; -.
DR   eggNOG; COG0845; Bacteria.
DR   HOGENOM; CLU_018816_2_0_6; -.
DR   Proteomes; UP000022611; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022611}.
FT   DOMAIN          68..115
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   REGION          372..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  41701 MW;  58A4746934B05944 CRC64;
     MLMPIPGKKL LIAALLVTVT AVAIGVAFKP ATSKLSAPTA IPVRVVSVVE RDVPRYVSAI
     GSVLSLHSVV IRPQIDGILT RLLVKEGQLV KAGDLLATID DRSIRASLDQ ARAQLGENQA
     QLQVAQVNLK RYKLLSVDDG VSKQTYDQQQ ALVNQLKATA QGNQAAIDAA QVQLSYTQIR
     SPVTGRVGIR TVDEGNFLRM SDTQGLFSVT QIDPIAVEFS LPQQMLPTLQ RLISATPPAD
     VNAYLGADTN GQTGDLLGEG HLTLIDNQIN ANTGTIRAKA EFSNAGQKLW PGQLVTLKIQ
     TAVDKHALVV PPSVVQRGLD QHFVYRVSGN KVESVPVQMV YQDSGLNIIT GVQAGDVLVS
     DGQSRLKPGA SVQILGEPPA LTQSTAAERQ P
//
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