ID A0A1J4WRU8_9BACT Unreviewed; 546 AA.
AC A0A1J4WRU8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Membrane fusion protein biotin-lipoyl like domain-containing protein {ECO:0000259|Pfam:PF13533};
GN ORFNames=AUJ34_01610 {ECO:0000313|EMBL:OIO49245.1};
OS Parcubacteria group bacterium CG1_02_41_12.
OC Bacteria.
OX NCBI_TaxID=1805307 {ECO:0000313|EMBL:OIO49245.1, ECO:0000313|Proteomes:UP000183016};
RN [1] {ECO:0000313|EMBL:OIO49245.1, ECO:0000313|Proteomes:UP000183016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_41_12 {ECO:0000313|EMBL:OIO49245.1};
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:OIO49245.1}.
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DR EMBL; MNWH01000033; OIO49245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4WRU8; -.
DR STRING; 1805307.AUJ34_01610; -.
DR Proteomes; UP000183016; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 6.20.50.140; -; 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..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..104
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 123..150
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 546 AA; 59440 MW; 1C767833C22DAC7F CRC64;
MIKKVIIGII ILMIGGMVLW FLKFRTTQGP EYVTETAQIG TLTQSVEATG KVESMQRIDL
NFKAGGRIEQ MNVKVGDKVR SGQVLARLDS RALMSRISDA QAEVDKQKAD YEKLVAGASD
TDIKVTEDTV AQKQQDVASA ENSLVNLRAK RKTELDNLKE KAITVLKNEV LVCQLAIEVI
NNTLDDPSAN NSYAYISTDK QKAQLSKNSA NIEISAVESS SGELSVISGD TDILSNLDDG
KLMLDSVKTA LTDTMSVLNN ANTTYSFLES DLDTLKSSIQ AQQATINTSR TNIVAAKTNW
TDKIAYYNDQ IAAAEDSVSQ AESALTVAQS QLDLKKSPPR KFEIDAQNAR VAQAQASLSL
ALANMEESII RAPLVGTITK KYYEAGEQTS LSSPVLEMIG EATLEIEVDI PESDISKIII
GQETKITLDA FGDEREYTGS VTFVDPAETL ISDVVYYRVK AAFSDSGQVK PGMTANVTII
TDMKENALYV PVRAVKSRNG DKYIEVLENG LVVEKIITLG LRGDEGIEIL SGLEEGDEVI
TFVKEK
//
