ID   A0A1G2IWR5_9BACT        Unreviewed;       551 AA.
AC   A0A1G2IWR5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Membrane fusion protein biotin-lipoyl like domain-containing protein {ECO:0000259|Pfam:PF13533};
GN   ORFNames=A2358_03975 {ECO:0000313|EMBL:OGZ79113.1};
OS   Candidatus Staskawiczbacteria bacterium RIFOXYB1_FULL_37_44.
OC   Bacteria; Candidatus Staskawiczbacteria.
OX   NCBI_TaxID=1802223 {ECO:0000313|EMBL:OGZ79113.1, ECO:0000313|Proteomes:UP000178650};
RN   [1] {ECO:0000313|EMBL:OGZ79113.1, ECO:0000313|Proteomes:UP000178650}
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:OGZ79113.1}.
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DR   EMBL; MHPJ01000009; OGZ79113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2IWR5; -.
DR   STRING; 1802223.A2358_03975; -.
DR   Proteomes; UP000178650; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
PE   4: Predicted;
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        21..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          77..122
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   REGION          529..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          108..135
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        529..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  59361 MW;  DDB21166DF0B39E3 CRC64;
     MINIIKKIAS VIKVFTLKHK IISLIIILCL LGGGFWIYKS LTNNDGQTSY VLGAVAKGTI
     ISSISGTGQV SAFDKIDVKP KVSGKIVYIN IQKDNEIKAG TFLAQIDARD AQSAVQSAEN
     DLDSARLSLT DINGEAKDAL DAAYDKGLDA LTTTYKDLAS MKANLDSMFL ESSYNGNDSD
     INYYLDFVRF YDEKTNDLSF WITDAKQKYS DMQKNMDTVE EIGWTISKNS QASQIENIVA
     ETYNSVKIFL DLIRQTSNLT QRYQKISETK NLTTPIKTAA TTTQITQLSA ALEALIKDTA
     TLLTAKSDIT AKKVALSKAN IDIKSQNLSM QKYENALLDA KENLAKYYIY SSIDGIISAV
     DSTIKTGDII SSGIVLGSIV TKQQVIEISL NEVDAVKVKT GQKVTIAFDA LPDITATGSV
     VDVDIVGVVS QGVVSYGVKI ALDIIDSQIK PGMSGSVNII TETKQNVLTV PNGAVKSKNE
     AYYVLVPGSP APIQKTVEVG VADDTNTEII SGLAEGDQIV IRTISNSKSA TPTIPSTTRQ
     ATQGLFGPGG R
//