ABC1_AJECA
ID ABC1_AJECA Reviewed; 1327 AA.
AC B2KWH4;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=ABC transporter 1 {ECO:0000303|PubMed:18404210};
DE AltName: Full=Siderophore biosynthesis cluster protein ABC1 {ECO:0000303|PubMed:18404210};
GN Name=ABC1 {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).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 26032 / G217B;
RX PubMed=18549241; DOI=10.1021/bi800066s;
RA Chao L.Y., Marletta M.A., Rine J.;
RT "Sre1, an iron-modulated GATA DNA-binding protein of iron-uptake genes in
RT the fungal pathogen Histoplasma capsulatum.";
RL Biochemistry 47:7274-7283(2008).
CC -!- FUNCTION: ABC transporter; part of the gene cluster that mediates the
CC biosynthesis of hydroxamate-containing siderophores that play a
CC critical role in virulence via intracellular iron acquisition during
CC macrophage infection (PubMed:18404210). Probably involved in the
CC excretion of the extracellular siderophores (PubMed:18404210).
CC {ECO:0000269|PubMed:18404210}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced during iron deprivation
CC (PubMed:18404210). {ECO:0000269|PubMed:18404210}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; EU253969; ACC64447.1; -; Genomic_DNA.
DR AlphaFoldDB; B2KWH4; -.
DR SMR; B2KWH4; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1327
FT /note="ABC transporter 1"
FT /id="PRO_0000444420"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 743..763
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 785..805
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 859..881
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 888..910
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 971..991
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1005..1025
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 47..326
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 386..663
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 743..1031
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1084..1323
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1054..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 421..428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1119..1126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1050
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1327 AA; 142704 MW; DEB33DA3EF00AED1 CRC64;
MTEASEDLAA GESKTAKSRR IIRRATRYVR LLVYAEPTTV DLILLTLGIL AAIASGVPFP
LMGIIFGQLV DNLNSASCNT DSQRGSAYQS EVNDKALKVV YVGIAYFVLV YIYIASWNLF
GERLAQRLRE RYFKSLLRQD ASFFDNMPAG EAASRLTSDI TTIQQGTSEK VGIVLNSVSF
FITAYIIAFV KDAKLGGELV SLTPAYLLMS LVGGYYTQKY ASAMLKNVAG ASSVAMEALS
NATIVHAFSA NAQLESKFAG LLGNAKVAGI RKAISVAVQS GLLYFIAFSA NGLAFWQGSK
TIADAVASGN PGSSVGTTYT VIFLLVDGEI FNIKVSSIRQ VAPFVQVFDA AGVTFESLEA
DINREPKIDG TVEGTENSLR NVSGNIELNN VSFAFPSRPD KPVLDNVSMS CAAGQHTAIV
GLSGSGKSTV AGLIARLYDP TNGEVSFAGQ NIKDLNVRSL RSNLSLVQQE PSLLDRSILE
NIALGLINSP SHSHLSPALL GGKLSDIATA VRNGRDLMEE AEIHGQETAE IIDMVRNAAD
LADASAFIGR LKDGYGTLVG SAGSLISGGQ KQRISIARSL VKKPKLLILD EATAALDSTS
QQRVQSAIEK VMSGRTLISI AHRLSTIKNA DNIIVMNQGK VVEQGTHSEL ISSDGAYAGL
VRLQNLNIRP EEENVSSESL ATKDSYDNII EKAAEASLDE RRSLETSARK GEDNSDGINA
KRSLSSTLKA VGPMLRPHML FLFLALTSAF VVGGTYSASA VVFGNTIGGL SPCKTADSIR
SAGKFYGLMF FILAIIEFFA NLGSWSAFGW VAEKITYKVR VLSFRALMEQ DLQWHQSDGR
SPTVLLSIIT QDGNALSGLT GSVVGTIIAI LVNLVVAIAL SHVIAWKIAL VCLAVVPLML
GAGVMRVITM TQFQERHARA FEKSLGITVE AVNSIKTISA LSLEHEILRT YRRSLKGPTM
EIAQQSAYAN LWLAISYGVS NFLYALAYWW GAKRIIAGDY SQTQFFIVLM ALLVSAQLWG
QMFTLAPDVS RAFTALARIL NLLDLGSTKN LSGPCQHLKP GNDLEANAEP REKRPDQSQG
GISVSLNNVK FSYPARQDVL VLDGLDIHIK PGQFAALVGP SGAGKSTIVS LIERLYTPTS
GSVHIDGQDI SAREGVSFRD NIAFVPQDSV LFEGTIRFNV ALGARPGHKP TDAEIEEACR
LANIHDTIVN LPEGYNTNCG PSGNQLSGGQ KQRLAIARAL VRKPQLLLLD ESTSALDAES
EQLLQAGLEK ATKGMTVIAI AHRLYTIQKA DVIFLIEDGR CTDKGTHAEL VERSESYKIN
ALHQAFE
