ID A0A1J5FKU9_9BACT Unreviewed; 548 AA.
AC A0A1J5FKU9;
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=AUK13_01475 {ECO:0000313|EMBL:OIP56262.1};
OS Candidatus Kuenenbacteria bacterium CG2_30_39_24.
OC Bacteria; Candidatus Kuenenbacteria.
OX NCBI_TaxID=1805236 {ECO:0000313|EMBL:OIP56262.1, ECO:0000313|Proteomes:UP000183922};
RN [1] {ECO:0000313|EMBL:OIP56262.1, ECO:0000313|Proteomes:UP000183922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_39_24 {ECO:0000313|EMBL:OIP56262.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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:OIP56262.1}.
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DR EMBL; MNYR01000021; OIP56262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5FKU9; -.
DR STRING; 1805236.AUK13_01475; -.
DR Proteomes; UP000183922; 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 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 5..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..102
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 122..156
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 311..364
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 548 AA; 58638 MW; F041A6D8E5E141EB CRC64;
MKKKIIIASI IVILVIAIIV VVISGKSKPE YVTAPAEIGN VVQSVDATGV VSSAEDIELN
FKITGLISSI HVKKADKVSA GQILAALDAG ALNSRVADAR GELLEAGANL KKVLAGSTPE
DVKISEITVE QKKQNLNSAQ NNLDNLKLQR DTELQNLKNT AIVTFNNELI DAESAMETVD
QTLDSADAQE TLGILKSGAV DKAEESQVVA ETAVAQTKLA VASIIRSSTD AQVLTAINQV
MAALDDVRAC LSDVFDVLQN TIISSSLSQT ELDALISGIQ TEQTTISTSK INIQTAESNW
TNKIVYYADQ ITKAEDEAAA AEDSFELAQA QLALKEAQPQ DYDITAANAR VTKAEASLAL
AQANLNDTII RAPVAGTIME INSKIGESTS LATPVIKMIG ESELEIEVDI PESDITKIEV
GQSAEITLDS FSDDNLFSGT VTFIDPAETV IQDVVYYQVT VQFSDGQDNI KPGMTANVTI
KTKEKSNVLR VPLRSVKQNN GDKIVEMLEG EQIKEHPVTS GLRGDEYYEI LDGLSAGEQV
ITFIKNGK
//
