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Database: UniProt
Entry: A0A1F4Q309_9BACT
LinkDB: A0A1F4Q309_9BACT
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ID   A0A1F4Q309_9BACT        Unreviewed;       408 AA.
AC   A0A1F4Q309;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Membrane fusion protein biotin-lipoyl like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A3H39_09335 {ECO:0000313|EMBL:OGB90345.1};
OS   candidate division NC10 bacterium RIFCSPLOWO2_02_FULL_66_22.
OC   Bacteria; candidate division NC10.
OX   NCBI_TaxID=1801658 {ECO:0000313|EMBL:OGB90345.1, ECO:0000313|Proteomes:UP000177374};
RN   [1] {ECO:0000313|EMBL:OGB90345.1, ECO:0000313|Proteomes:UP000177374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the UPF0194 family.
CC       {ECO:0000256|ARBA:ARBA00010602}.
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:OGB90345.1}.
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DR   EMBL; METH01000177; OGB90345.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4Q309; -.
DR   STRING; 1801658.A3H39_09335; -.
DR   Proteomes; UP000177374; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.40.30.170; -; 1.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 1.10.287.470; Helix hairpin bin; 2.
DR   InterPro; IPR032317; HlyD_D23.
DR   InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR   PANTHER; PTHR32347; EFFLUX SYSTEM COMPONENT YKNX-RELATED; 1.
DR   PANTHER; PTHR32347:SF23; UPF0194 MEMBRANE PROTEIN YBHG; 1.
DR   Pfam; PF13533; Biotin_lipoyl_2; 1.
DR   Pfam; PF16576; HlyD_D23; 1.
DR   PRINTS; PR01490; RTXTOXIND.
DR   SUPFAM; SSF111369; HlyD-like secretion proteins; 3.
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        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          49..94
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   DOMAIN          237..353
FT                   /note="RND efflux pump membrane fusion protein barrel-
FT                   sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF16576"
FT   COILED          81..163
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          217..275
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   408 AA;  44559 MW;  1252387AD6229E19 CRC64;
     MTHPPRPIMI IGTGIIVAGL AAGGWSWWRS RQDARDVIQA SGRIEVTEVS VSSKVTGRVA
     KLSVEEGTDV RLGQPIADLE GEELEAQLRQ ARAAMQSAEA KLNQARITLR VEPVTIRTQI
     RQAEENLRAA EERLRMLRAG FRVQEIEEGR ANLHQNLARL EIARLTRDRF RELLADGAIS
     KQELDRAESD FQAAGAAVRA TRERLAMLVE GARSEDIRMA EAERDRAGAA LEAARANAAT
     LDLRQQDVRV AEAAVREAAA NVRRLETQVA ELKVVAPMDA TVLTKAVEVG EVVAAGKPLV
     LLGDLDHPWI KIYVSETALG KVMLGAPARV LVDSFPGQPF QGTVTWISDQ AEFTPKNVQT
     AEERVNLVYA VKITIASAER KLKAGMPADA VLPLTTPSPH SPTGERRR
//
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