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Database: UniProt
Entry: A0A0A7S645_FRIPE
LinkDB: A0A0A7S645_FRIPE
Original site: A0A0A7S645_FRIPE 
ID   A0A0A7S645_FRIPE        Unreviewed;       391 AA.
AC   A0A0A7S645;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Multidrug resistance efflux pump {ECO:0000313|EMBL:AJA44756.1};
GN   ORFNames=FPB0191_00930 {ECO:0000313|EMBL:AJA44756.1};
OS   Frischella perrara.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Orbales; Orbaceae;
OC   Frischella.
OX   NCBI_TaxID=1267021 {ECO:0000313|EMBL:AJA44756.1, ECO:0000313|Proteomes:UP000030901};
RN   [1] {ECO:0000313|EMBL:AJA44756.1, ECO:0000313|Proteomes:UP000030901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEB0191 {ECO:0000313|EMBL:AJA44756.1,
RC   ECO:0000313|Proteomes:UP000030901};
RX   PubMed=25527542;
RA   Engel P., Vizcaino M.I., Crawford J.M.;
RT   "Gut symbionts from distinct hosts exhibit genotoxic activity via divergent
RT   colibactin biosynthetic pathways.";
RL   Appl. Environ. Microbiol. 0:0-0(2014).
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; CP009056; AJA44756.1; -; Genomic_DNA.
DR   RefSeq; WP_039104368.1; NZ_QGTI01000023.1.
DR   AlphaFoldDB; A0A0A7S645; -.
DR   STRING; 1267021.FPB0191_00930; -.
DR   GeneID; 78459363; -.
DR   KEGG; fpp:FPB0191_00930; -.
DR   HOGENOM; CLU_023976_8_0_6; -.
DR   OrthoDB; 9775513at2; -.
DR   Proteomes; UP000030901; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR   Gene3D; 2.40.30.170; -; 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; IPR006144; Secretion_HlyD_CS.
DR   PANTHER; PTHR30386:SF25; MEMBRANE FUSION PROTEIN (MFP) FAMILY PROTEIN; 1.
DR   PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR   Pfam; PF13533; Biotin_lipoyl_2; 1.
DR   Pfam; PF13437; HlyD_3; 1.
DR   PRINTS; PR01490; RTXTOXIND.
DR   SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
DR   PROSITE; PS00543; HLYD_FAMILY; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030901};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..105
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
SQ   SEQUENCE   391 AA;  43685 MW;  6B8F7AA755E6E9B2 CRC64;
     MSKRSINNWD IVEGGTSKSQ LLIWFIVLAI SCFYVWASVF KLTEVSSGTG KVIASSKEQV
     IQSLEGGVLK QLNVKEGQLV EANQVLAFID PTRMQSSVGE AQAKLKAAKA TVARLRAEVD
     ETPLVFPEEV LNDSSLVKYE SNLFESRRKS LTESIEGIKQ SQQLILQELK LTEPLVLKGA
     ASNVEILRLK RQLNELKSKE IDIKGQYIVK AREELAKATA EVGSQMEILR GRQDALMRTT
     IESPVRGIVK NIAISTLGGV IPPGGRLMEI IPVDERLQIE ARISPRDIAY IRDGLPAIVR
     ITAYDYSIYG ALNGVVETIS PDTIQDEVNR DNYYYRVYIK TDSDQLMDKN GVAHIIKPGM
     IATVDIRTGE KTVLEYLIKP FNKMREAMRE R
//
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