IRTB_MYCT3
ID IRTB_MYCT3 Reviewed; 579 AA.
AC G7CBF6;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Mycobactin import ATP-binding/permease protein IrtB {ECO:0000305};
DE EC=7.2.2.- {ECO:0000269|PubMed:32296173};
GN Name=irtB {ECO:0000303|PubMed:32296173};
GN ORFNames=KEK_01490 {ECO:0000312|EMBL:EHI14681.1};
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 (2.7 ANGSTROMS) OF THE IRTAB COMPLEX, FUNCTION,
RP ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND 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). 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 -!- 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 -!- SUBUNIT: Forms a heterodimer with IrtA. {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 IrtB the ATP-binding domain (NBD) and the transmembrane
CC domain (TMD) are fused (PubMed:32296173). The IrtAB transporter assumes
CC an inward-facing conformation, which may represent the low-affinity
CC state after mycobactin release towards the SID and the cytoplasm
CC (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}.
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DR EMBL; AGVE01000012; EHI14681.1; -; Genomic_DNA.
DR RefSeq; WP_003923707.1; NZ_AGVE01000012.1.
DR PDB; 6TEJ; X-ray; 2.70 A; B=2-579.
DR PDBsum; 6TEJ; -.
DR AlphaFoldDB; G7CBF6; -.
DR SMR; G7CBF6; -.
DR STRING; 1078020.KEK_01490; -.
DR EnsemblBacteria; EHI14681; EHI14681; KEK_01490.
DR PATRIC; fig|1078020.3.peg.288; -.
DR eggNOG; COG1132; Bacteria.
DR OMA; MQVPGQL; -.
DR OrthoDB; 643917at2; -.
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 Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..579
FT /note="Mycobactin import ATP-binding/permease protein IrtB"
FT /id="PRO_0000450629"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 47..48
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 70..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 169..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 263..272
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 294..579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32296173"
FT DOMAIN 21..299
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 332..565
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 364..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 579 AA; 60704 MW; 375637F694D78916 CRC64;
MIRTLLRLVP AEKRGAVAGY AVLTLLSVLL RAVGAVLLIP LLAALFSDTP SDAWLWLGWL
TAVTLAGWVT DTNTARLGFD LGFAVLSRTQ HDMADRLPNV AMSWFTPDNT ATARQAIAAT
GPELAGLVVN LLTPLIGAAL LPAAIGVALL FVSVPLGLAA LAGVAVLFGA LALSGRLSRA
ADKVAGETNS AFTERIIEFA RTQQALRAAR RVEPARSQVG SALAAQHGAG LRLLTMQIPG
QVLFSLAGQV ALIGFAGMAV WLTVRGQLGV PEAIALIVVL VRYLEPFAAI ADLAPALETT
RATLNRIQAV LDAPTLPAGR RRLDRTGAAP SIEFDDVRFS YGDEVVLDGV SFTLRPGNTT
AIVGPSGSGK TTILSLIAGL QQPASGRVLL DGVDVTTLDP EARRAAVSVV FQHPYLFDGT
LRDNVLVGDP EADPDDVTAA MRLARVDELL DRLPDGDATV VGEGGTALSG GERQRVSIAR
ALLKPAPVLL VDEATSALDN ANEAAVVDAL TADPRPRTRV IVAHRLASIR HADRVLFVEA
GRVVEDGAID ELLAAGGRFA QFWAQQQAAS EWAIGSTAR
