ID   A0A1F8QQG7_9CHLR        Unreviewed;       542 AA.
AC   A0A1F8QQG7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Membrane fusion protein biotin-lipoyl like domain-containing protein {ECO:0000259|Pfam:PF13533};
GN   ORFNames=A2147_07995 {ECO:0000313|EMBL:OGO37669.1};
OS   Chloroflexi bacterium RBG_16_57_8.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797652 {ECO:0000313|EMBL:OGO37669.1, ECO:0000313|Proteomes:UP000178359};
RN   [1] {ECO:0000313|EMBL:OGO37669.1, ECO:0000313|Proteomes:UP000178359}
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   -!- 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:OGO37669.1}.
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DR   EMBL; MGNT01000120; OGO37669.1; -; Genomic_DNA.
DR   Proteomes; UP000178359; Unassembled WGS sequence.
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   PANTHER; PTHR32347; EFFLUX SYSTEM COMPONENT YKNX-RELATED; 1.
DR   PANTHER; PTHR32347:SF14; EFFLUX SYSTEM COMPONENT YKNX-RELATED; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..542
FT                   /note="Membrane fusion protein biotin-lipoyl like domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009538113"
FT   DOMAIN          61..105
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   REGION          413..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          98..259
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        518..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  56991 MW;  CBB53F3408C38C51 CRC64;
     MKLARILVAT VAGGVLAASL AGCGAKASST PKSQIATVQR GDITVSITGT GNLAYSKTAD
     LAFEMAGIVQ EVLVEEGEIV TEGQKLAGLD GTEWDDQVNM MEKALTAAQR NLKSAERQIT
     AKELAVRQVE LDLQSAEDNV ADIPAVKAAX XXVDMAESAL TAAQATYGAN PSFTGTQLQA
     IQQQLADAKR NLQEVLAGTS FNTTSDMALQ ISKANLKVEQ VQRQLEDAKI AVEDANLAKT
     EAEQSLEDAQ NDLDEAKGLT PAIVAPFAGV VTSVKVEGGA EVKKGAVAVQ IADPTKFEAN
     ILVGENDIFQ VKLDGDATVQ VDSLSGLSLP AKVTYVAPTA TVQQGVVNYK VMVELQSLEE
     IAQQRQQATQ GAGQADASTQ LSERLKQAVQ SGRMTQEQAD AFLKQMQEGG SAFFQQGTSG
     SQSPFGQRFQ QGAAAPESFQ LRQGLSVTVN IVTAERNNVL LVPNDAVTRK AGATLVNVQA
     NGSTEQRQVT CGISDWQHTE IINGLTEGDQ VVITKSTSTS ASGSNQGSQQ RFGVPGGGFM
     IR
//