IRTA_MYCS2
ID IRTA_MYCS2 Reviewed; 860 AA.
AC A0R6H8; I7FV42;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 OrderedLocusNames=MSMEG_6554 {ECO:0000312|EMBL:ABK72388.1},
GN MSMEI_6377 {ECO:0000312|EMBL:AFP42803.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ARG-55; GLN-234 AND ARG-241.
RC STRAIN=ATCC 700084 / mc(2)155;
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:0000250|UniProtKB:G7CBF5};
CC -!- SUBUNIT: Forms a heterodimer with IrtB. {ECO:0000269|PubMed:32296173}.
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:0000269|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}.
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DR EMBL; CP000480; ABK72388.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42803.1; -; Genomic_DNA.
DR RefSeq; WP_011731355.1; NZ_SIJM01000033.1.
DR RefSeq; YP_890766.1; NC_008596.1.
DR AlphaFoldDB; A0R6H8; -.
DR SMR; A0R6H8; -.
DR STRING; 246196.MSMEI_6377; -.
DR PRIDE; A0R6H8; -.
DR EnsemblBacteria; ABK72388; ABK72388; MSMEG_6554.
DR EnsemblBacteria; AFP42803; AFP42803; MSMEI_6377.
DR GeneID; 66737821; -.
DR KEGG; msg:MSMEI_6377; -.
DR KEGG; msm:MSMEG_6554; -.
DR PATRIC; fig|246196.19.peg.6378; -.
DR eggNOG; COG1132; Bacteria.
DR eggNOG; COG2375; Bacteria.
DR OMA; GAYLEGQ; -.
DR OrthoDB; 643917at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; FAD; Flavoprotein;
KW Membrane; Nucleotide-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..860
FT /note="Mycobactin import ATP-binding/permease protein IrtA"
FT /id="PRO_0000450628"
FT TOPO_DOM 1..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 315..335
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 357..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 431..433
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 455..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 547..550
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 572..860
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 15..124
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 295..577
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 609..842
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 242..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..259
FT /note="Basic and acidic residues"
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 238..240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:G7CBF5"
FT BINDING 642..649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 55
FT /note="R->E: Cannot reduce Fe(III)-cMBT and Fe(III)-MBT;
FT when associated with E-234 and E-241."
FT /evidence="ECO:0000269|PubMed:32296173"
FT MUTAGEN 234
FT /note="Q->E: Cannot reduce Fe(III)-cMBT and Fe(III)-MBT;
FT when associated with E-55 and E-241."
FT /evidence="ECO:0000269|PubMed:32296173"
FT MUTAGEN 241
FT /note="R->E: Cannot reduce Fe(III)-cMBT and Fe(III)-MBT;
FT when associated with E-55 and E-234."
FT /evidence="ECO:0000269|PubMed:32296173"
SQ SEQUENCE 860 AA; 93263 MW; E80AABC055D7CBF0 CRC64;
MARGIQGVMM RGFGARDHQA TVVSTEAITP NLLRLRMVSP TLFEDAVAEP TSWLRFWFPD
PAGSKTEFQR AYTMSEMSPE TGEFAIDVVL HEPAGPASRW ARSAKPGDAI AVMTLGSAGF
SVPEDPPAGY LLIGDAAATP AINGIIGVVP HDIPIEVYLE EHDENDRLIP IAEHPRMRVH
WVVREDATSL AGAIEARDWS NWYCWVTPEA GSLKHLRTRL RDEFGFPKAE LHPQAYWTEG
RAMGTKRGDD DKTPEVNPAP RADKPEAPAP AAAGRGNWRA QAAGRLLAPL KTTLIISGVL
QAIITLVQLA PFVLLVELAR LLLSGASSDR LWTLGVVAIS LLGTGSFLAA ALTLWLHLVD
ARFARDLRTG LLTKMSRLPL GWFTARGSGS IKQLVQDDTL SLHYLITHAI PDAVAAVIAP
VAVLVYLFVV DWRLALVMFV PVLIYLVLMT VMTIQSGPKI AQSQRWAERM SAEAGAYLEG
QPVVRVFGGA AASSFRRRLD EYIGFLVAWQ KPFTGKKSMM DLVTRPGTFL WLIVAVGTPM
ITSGAMDPVD ILPFLLLGTT FGVRLLGIAY GLGGIRGGML AARRIQTTLD ETELVIREQT
GKRDGEPAVV FDNVTFGYRP DIPVLHDISL QLTPGTVTAL VGPSGSGKST LAALLARFHD
VDAGAIRLGG RDIRTLTADE LYRQVGFVLQ DTQLVGGTVA ENIALADPDA SIERIQDAAR
DAQIHDRIMR LPNGYDTPLG AASSLSGGEK QRLTIARAIL ADTPVLILDE ATAFADPESE
YLVQQALNRL TRDRTVLVIA HRLHTITHAD QIVVLEGGRI VETGTHERLL DAAGRYRQLW
ETGQRPALAT AAGPTGEAVR
