RTA1_AJECA
ID RTA1_AJECA Reviewed; 312 AA.
AC B2KWI0;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Lipid-translocating exporter-like protein RTA1 {ECO:0000305|PubMed:18404210};
DE AltName: Full=Siderophore biosynthesis cluster protein RTA1 {ECO:0000303|PubMed:18404210};
GN Name=RTA1 {ECO:0000303|PubMed:18404210};
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 26032 / G217B;
RX PubMed=18404210; DOI=10.1371/journal.ppat.1000044;
RA Hwang L.H., Mayfield J.A., Rine J., Sil A.;
RT "Histoplasma requires SID1, a member of an iron-regulated siderophore gene
RT cluster, for host colonization.";
RL PLoS Pathog. 4:E1000044-E1000044(2008).
CC -!- FUNCTION: Lipid-translocating exporter-like protein; part of the gene
CC cluster that mediates the biosynthesis of hydroxamate-containing
CC siderophores that play a critical role in virulence via intracellular
CC iron acquisition during macrophage infection (PubMed:18404210).
CC {ECO:0000269|PubMed:18404210}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:18404210}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression seems not to be induced during iron deprivation
CC (PubMed:18404210). {ECO:0000269|PubMed:18404210}.
CC -!- SIMILARITY: Belongs to the lipid-translocating exporter (LTE) (TC
CC 9.A.26.1) family. {ECO:0000305}.
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DR EMBL; EU253975; ACC64453.1; -; Genomic_DNA.
DR AlphaFoldDB; B2KWI0; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR007568; RTA1.
DR PANTHER; PTHR31465; PTHR31465; 1.
DR Pfam; PF04479; RTA1; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..312
FT /note="Lipid-translocating exporter-like protein RTA1"
FT /id="PRO_0000444419"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 312 AA; 34277 MW; ADCC1F28B6530136 CRC64;
MSPESKKITA HGSTSMPLSR TSKPQKFTIP LTVGAIFSVI GFLQRFFLAS GKGDVQSLYT
LSTMFILGAG PTYAGADYFI CGRLFSFVPS AAPMSPIRVV RTFITFDVLA EVCVWTGAGL
LAGAHTDTAA RYKIGLNLIR AAMITQAFLF TSFVAILASF HVRVCALRAE WSVTSNGGTG
RRFMMVVHSL YASSIFIIIR SAYHIAGHSF RTNEQPFLIC EASLMLLNTA MFNVFHPGHI
LPIDSRVYVG IDGQERANET IEGAFTDSRP LLQKILDPLD VKGLFSRDKK RWHDPTAELE
MDINSTLYAA LT