IRTA_MYCTO
ID IRTA_MYCTO Reviewed; 859 AA.
AC P9WQJ8; L0T6D6; P63391; Q11018;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Mycobactin import ATP-binding/permease protein IrtA {ECO:0000250|UniProtKB:G7CBF5};
DE EC=7.2.2.- {ECO:0000250|UniProtKB:G7CBF5};
DE AltName: Full=Iron-regulated transporter A;
GN Name=irtA; OrderedLocusNames=MT1390;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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). Mycobactins are then reduced by the siderophore interaction
CC domain to facilitate iron release in the bacterial cell. Transmembrane
CC domains (TMD) form a pore in the membrane and the ATP-binding domain
CC (NBD) is responsible for energy generation.
CC {ECO:0000250|UniProtKB:G7CBF5}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:G7CBF5};
CC -!- SUBUNIT: Forms a heterodimer with IrtB. {ECO:0000250|UniProtKB:G7CBF5}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:G7CBF5}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:G7CBF5}.
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.
CC {ECO:0000250|UniProtKB:G7CBF5}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Siderophore-
CC Fe(3+) uptake transporter (SIUT) (TC 3.A.1.21) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK45654.1; -; Genomic_DNA.
DR PIR; C70740; C70740.
DR RefSeq; WP_003406958.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQJ8; -.
DR SMR; P9WQJ8; -.
DR PRIDE; P9WQJ8; -.
DR EnsemblBacteria; AAK45654; AAK45654; MT1390.
DR KEGG; mtc:MT1390; -.
DR PATRIC; fig|83331.31.peg.1498; -.
DR HOGENOM; CLU_000604_33_1_11; -.
DR Proteomes; UP000001020; Chromosome.
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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; FAD; Flavoprotein;
KW Membrane; Nucleotide-binding; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..859
FT /note="Mycobactin import ATP-binding/permease protein IrtA"
FT /id="PRO_0000426763"
FT TOPO_DOM 1..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 314..334
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 356..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 430..432
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 454..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 541..548
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 570..859
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 15..122
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 293..575
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 610..843
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 247..267
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:0000250|UniProtKB:G7CBF5"
FT BINDING 87..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:G7CBF5"
FT BINDING 97..98
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:G7CBF5"
FT BINDING 643..650
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 859 AA; 92966 MW; 37D756CCB349C9BD CRC64;
MARGLQGVML RSFGARDHTA TVIETISIAP HFVRVRMVSP TLFQDAEAEP AAWLRFWFPD
PNGSNTEFQR AYTISEADPA AGRFAVDVVL HDPAGPASSW ARTVKPGATI AVMSLMGSSR
FDVPEEQPAG YLLIGDSASI PGMNGIIETV PNDVPIEMYL EQHDDNDTLI PLAKHPRLRV
RWVMRRDEKS LAEAIENRDW SDWYAWATPE AAALKCVRVR LRDEFGFPKS EIHAQAYWNA
GRAMGTHRAT EPAATEPEVG AAPQPESAVP APARGSWRAQ AASRLLAPLK LPLVLSGVLA
ALVTLAQLAP FVLLVELSRL LVSGAGAHRL FTVGFAAVGL LGTGALLAAA LTLWLHVIDA
RFARALRLRL LSKLSRLPLG WFTSRGSGSI KKLVTDDTLA LHYLVTHAVP DAVAAVVAPV
GVLVYLFVVD WRVALVLFGP VLVYLTITSS LTIQSGPRIV QAQRWAEKMN GEAGSYLEGQ
PVIRVFGAAS SSFRRRLDEY IGFLVAWQRP LAGKKTLMDL ATRPATFLWL IAATGTLLVA
THRMDPVNLL PFMFLGTTFG ARLLGIAYGL GGLRTGLLAA RHLQVTLDET ELAVREHPRE
PLDGEAPATV VFDHVTFGYR PGVPVIQDVS LTLRPGTVTA LVGPSGSGKS TLATLLARFH
DVERGAIRVG GQDIRSLAAD ELYTRVGFVL QEAQLVHGTA AENIALAVPD APAEQVQVAA
REAQIHDRVL RLPDGYDTVL GANSGLSGGE RQRLTIARAI LGDTPVLILD EATAFADPES
EYLVQQALNR LTRDRTVLVI AHRLHTITRA DQIVVLDHGR IVERGTHEEL LAAGGRYCRL
WDTGQGSRVA VAAAQDGTR
