ID A0A0Q7KH73_9ACTN Unreviewed; 537 AA.
AC A0A0Q7KH73;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Membrane fusion protein biotin-lipoyl like domain-containing protein {ECO:0000259|Pfam:PF13533};
GN ORFNames=ASD10_05095 {ECO:0000313|EMBL:KQX74609.1};
OS Aeromicrobium sp. Root472D3.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736540 {ECO:0000313|EMBL:KQX74609.1, ECO:0000313|Proteomes:UP000050971};
RN [1] {ECO:0000313|EMBL:KQX74609.1, ECO:0000313|Proteomes:UP000050971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root472D3 {ECO:0000313|EMBL:KQX74609.1,
RC ECO:0000313|Proteomes:UP000050971};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX74609.1, ECO:0000313|Proteomes:UP000050971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root472D3 {ECO:0000313|EMBL:KQX74609.1,
RC ECO:0000313|Proteomes:UP000050971};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQX74609.1}.
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DR EMBL; LMET01000001; KQX74609.1; -; Genomic_DNA.
DR RefSeq; WP_056605594.1; NZ_LMET01000001.1.
DR AlphaFoldDB; A0A0Q7KH73; -.
DR STRING; 1736540.ASD10_05095; -.
DR OrthoDB; 5141338at2; -.
DR Proteomes; UP000050971; Unassembled WGS sequence.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.420.20; -; 1.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 2.
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; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000050971};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..537
FT /note="Membrane fusion protein biotin-lipoyl like domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006314148"
FT DOMAIN 66..107
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT REGION 111..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 313..340
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 115..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 53076 MW; 5EA8BE6C205869F2 CRC64;
MRRRRLAAAA IAGVVLVGGG SVAYAQTQSG AGSYRTATVT TGDVDETMGL SGIITASDRQ
DLSFGAGGTV EKVSVEAGDV VRSGSTLATL DSTDLETAVT KAEATLAKAK AQLETDEASQ
ASTVTDSETP TAATPAKSTP AKSTPTSSTP TRSPALEEAL AKLATQQTDL TSAQSAATEA
ISASKSALAA QIEACKAAET EEPTPADGED EGEATGLSRG CSDALDAVQA AQDVVADQQD
TLQTALEALS TTLTAAVEAV GESSSTRSTP STPSAPDDAD ATPTTPTTPT TPSTSGSTPS
GSASGPTVTA ATLAQDQASI DTAEAQLTEA ERQLKSAELT APFAGEILSV SVVEGDVVAD
SDVVIVIKGD GATTVTTTVT LDQIQDVTVG QTASVTPAGA VEATGGTVSS IALLPDASSG
TSTYPVTIEL AEPVAAPEGS TASISVVTGR AESVLTVPSS AVSTTIRTTV SVLVDGRPVV
TPVTVGVVGA TRTEITDGLT RGQEIVLADL DADLPSGDST TTSLTGGGFP RGPGGRG
//
