IRTA_MYCT3
ID IRTA_MYCT3 Reviewed; 908 AA.
AC G7CBF5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Mycobactin import ATP-binding/permease protein IrtA {ECO:0000305};
DE EC=7.2.2.- {ECO:0000269|PubMed:32296173};
GN Name=irtA {ECO:0000303|PubMed:32296173};
GN ORFNames=KEK_01485 {ECO:0000312|EMBL:EHI14680.1};
OS Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS 105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1078020;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316;
RG Tuberculosis Structural Genomics Consortium;
RA Ioerger T.R.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF THE SID DOMAIN IN COMPLEX WITH FAD
RP AND OF THE IRTAB COMPLEX, FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP DOMAIN.
RX PubMed=32296173; DOI=10.1038/s41586-020-2136-9;
RA Arnold F.M., Weber M.S., Gonda I., Gallenito M.J., Adenau S., Egloff P.,
RA Zimmermann I., Hutter C.A.J., Huerlimann L.M., Peters E.E., Piel J.,
RA Meloni G., Medalia O., Seeger M.A.;
RT "The ABC exporter IrtAB imports and reduces mycobacterial siderophores.";
RL Nature 580:413-417(2020).
CC -!- FUNCTION: Part of the ABC transporter complex IrtAB involved in the
CC import of iron-bound mycobactin (Fe-MBT) and carboxymycobactin (Fe-
CC cMBT) (PubMed:32296173). Has a preference for Fe-MBT over Fe-cMBT
CC (PubMed:32296173). Mycobactins are then reduced by the siderophore
CC interaction domain to facilitate iron release in the bacterial cell
CC (PubMed:32296173). Transmembrane domains (TMD) form a pore in the
CC membrane and the ATP-binding domain (NBD) is responsible for energy
CC generation (PubMed:32296173). {ECO:0000269|PubMed:32296173}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:32296173};
CC -!- ACTIVITY REGULATION: The ATPase activity of IrtAB is stimulated more
CC than 38-fold in the presence of Fe-MBT, and more than 10-fold in the
CC presence of Fe-cMBT. {ECO:0000269|PubMed:32296173}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=185 uM for mycobactin {ECO:0000269|PubMed:32296173};
CC -!- SUBUNIT: Forms a heterodimer with IrtB. {ECO:0000269|PubMed:32296173}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:32296173}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:32296173}.
CC -!- DOMAIN: In IrtA the ATP-binding domain (NBD) and the transmembrane
CC domain (TMD) are fused. In addition, IrtA contains an N-terminal
CC siderophore interaction domain (SID) that binds FAD (PubMed:32296173).
CC The IrtAB transporter assumes an inward-facing conformation, which may
CC represent the low-affinity state after mycobactin release towards the
CC SID and the cytoplasm (PubMed:32296173). {ECO:0000269|PubMed:32296173}.
CC -!- MISCELLANEOUS: The import function of IrtAB is contradictory to
CC structural predictions, which suggest that it has an ABC exporter fold.
CC {ECO:0000305|PubMed:32296173}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Siderophore-
CC Fe(3+) uptake transporter (SIUT) (TC 3.A.1.21) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EHI14680.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AGVE01000012; EHI14680.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_040545965.1; NZ_AGVE01000012.1.
DR PDB; 6TEJ; X-ray; 2.70 A; A=316-890.
DR PDB; 6TEK; X-ray; 1.80 A; A/B=16-245.
DR PDBsum; 6TEJ; -.
DR PDBsum; 6TEK; -.
DR AlphaFoldDB; G7CBF5; -.
DR SMR; G7CBF5; -.
DR STRING; 1078020.KEK_01485; -.
DR EnsemblBacteria; EHI14680; EHI14680; KEK_01485.
DR PATRIC; fig|1078020.3.peg.287; -.
DR eggNOG; COG1132; Bacteria.
DR eggNOG; COG2375; Bacteria.
DR Proteomes; UP000004915; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
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; IPR013113; FAD-bd_9_SIP.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR007037; SIP_C.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08021; FAD_binding_9; 1.
DR Pfam; PF04954; SIP; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; FAD;
KW Flavoprotein; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..908
FT /note="Mycobactin import ATP-binding/permease protein IrtA"
FT /id="PRO_0000450627"
FT TOPO_DOM 1..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 351..371
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 393..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 466..469
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 491..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 579..586
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 608..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT DOMAIN 15..124
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 331..613
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 654..887
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 16..245
FT /note="Siderophore interaction domain"
FT /evidence="ECO:0000305"
FT REGION 245..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70..73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32296173"
FT BINDING 87..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32296173"
FT BINDING 97..98
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32296173"
FT BINDING 241..243
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32296173"
FT BINDING 687..694
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 908 AA; 98141 MW; 32F77BF931C1CD31 CRC64;
MARGFQGVML RGLGARDHQA TVVDKEYIAP HFVRVRLVSP TLFDEVIVEP TSWLRFWFPD
PDGSDTEFQR AYTITESDPE TGRFAVDMVL HEPAGPASTW ARTVEPGATI AVMSMGSRGF
SVPEDPEDRP VGYLLIGDSA STPAINGIIE VVPHDIPIEL YLEQHHDDDV LIPLAEHPRL
RVHRVSRDDA SSLAAALELR DWSNWYCWAG PEAGALKQVR TRLRDEFGFP KREVYAQAYW
TEGRAMGSSR GETSTPAKPA AKTAPAKAAA KPAAASGAGT PEHAAAPAAA TTGAPQAAPA
PGAAQPRTPV RGRWRAEAGS RLLAPLKKPL IVSGVLQALI TLIELAPFVL LVELARLLLG
GAEAERLWTL GLTAVSLIGL GAVLAAAMTL WLHRVDARFA HELRGRLLTK LSRLPLGWFT
RRGSASTKQL VQDDTLALHY LITHAIPDAV AAVVAPVAVL VYLFVADWRV ALVLFIPVLV
YLVLMSVMTI QSGSKIAQAP RWAERMGGEA GAFLEGQPVI RIFGGAAASR FRRRLDDYID
FLVSWQRPFV GKKTLMDLVT RPATFLWIIL VAGVPLVVTG RMDPVNLLPF LLLGTTFGAR
LLGIGYGLSG IQTGMLAARR IQTVLDEPEL VVRDRTGQAG TDHASGDQAR PGTVELDRVS
FEYRPGVPVI RDVTLTLRPG TVTALVGPSG SGKSTLAALV ARFHDVTQGA IRVDGRDIRT
LTADELYRRV GFVLQDAQLV HGSVAENIAL AEPDAGLERI RTAARDAQIH DRITRMPDGY
DSVLGAGSAL SGGERQRVTI ARAILADTPV LVLDEATAFA DPESEYLVQQ AINRLTRDRT
VLVIAHRLHT ITHADQIVVL DDGRIVEVGT HDELLAAGGR YRGLWDSGRY SSPDAGRPVS
ADAVEVGR
