ID A0A1G1XND0_9BACT Unreviewed; 611 AA.
AC A0A1G1XND0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Membrane fusion protein biotin-lipoyl like domain-containing protein {ECO:0000259|Pfam:PF13533};
GN ORFNames=A2Y82_01370 {ECO:0000313|EMBL:OGY41615.1};
OS Candidatus Buchananbacteria bacterium RBG_13_36_9.
OC Bacteria; Candidatus Buchananbacteria.
OX NCBI_TaxID=1797530 {ECO:0000313|EMBL:OGY41615.1, ECO:0000313|Proteomes:UP000176498};
RN [1] {ECO:0000313|EMBL:OGY41615.1, ECO:0000313|Proteomes:UP000176498}
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 -!- 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:OGY41615.1}.
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DR EMBL; MHHZ01000015; OGY41615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1XND0; -.
DR Proteomes; UP000176498; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 2.
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 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..116
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 102..155
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 611 AA; 67172 MW; 490038CA6AC5C9FC CRC64;
MNSKWIFDIF KRLIKKKSFW VITIIIIIAI IGIGKLTAPK KVEYVQEKVI KGRLVQTVSE
TGSVLAATNI NLNFKGTGTI VEMNIKEGDE VKKDDILARL DAGSLEIQVR QAQANLSIAQ
ANLNRLFAGA SREDIKVTQE TVNNAKIAYE NAQKDYEIMS VKLAADLKAY SEALNLAEKN
LTNTGNTITQ TVDDARQTLI TTIRSKANAA NTTLDFIDYQ FTNLGNVADY QAKINTWDYY
TQALEKQTDL NNILIYSDQT VAGKIDEATS LALGLLEDIN LSLNSLFNTI GSTMADARFS
QLKIDNDKAL VKAEQTTNSA NLSAVQAAEF AYKTAKLNAT SSTDTSTSNY NTAKANYDSA
IATHDSQLNA AQANIDSALG NYNLTKAQLD LKKAPARGVD IAYYQAQVDQ AKAALDLVLK
NLDDYTIYAP RDGLITFVNY KVGEQIGFGI TSITEAAKAV ISMISKDQYE IEVDVPESDI
VKVKVGNLAR ITLDAYGSDV VFDGTVMFID LAETNIQDVV YYKVKVEINP YDLEIKPGMT
ANVDIVTAEK NDVLIVPIRA IKETQDKKKY VEILSFGKPK QVFVEIGLRG DDGYEITSGL
NEGDQVIVYK K
//