IRTB_MYCTO
ID IRTB_MYCTO Reviewed; 579 AA.
AC P9WQJ6; L0T6L2; P63393; Q11019;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Mycobactin import ATP-binding/permease protein IrtB {ECO:0000250|UniProtKB:G7CBF6};
DE EC=7.2.2.- {ECO:0000250|UniProtKB:G7CBF6};
DE AltName: Full=Iron-regulated transporter B;
GN Name=irtB; OrderedLocusNames=MT1392;
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). Transmembrane domains (TMD) form a pore in the membrane and the
CC ATP-binding domain (NBD) is responsible for energy generation.
CC {ECO:0000250|UniProtKB:G7CBF6}.
CC -!- SUBUNIT: Forms a heterodimer with IrtA. {ECO:0000250|UniProtKB:G7CBF6}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:G7CBF6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:G7CBF6}.
CC -!- DOMAIN: In IrtB the ATP-binding domain (NBD) and the transmembrane
CC domain (TMD) are fused. {ECO:0000250|UniProtKB:G7CBF6}.
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; AE000516; AAK45655.1; -; Genomic_DNA.
DR PIR; D70740; D70740.
DR RefSeq; WP_003900322.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQJ6; -.
DR SMR; P9WQJ6; -.
DR EnsemblBacteria; AAK45655; AAK45655; MT1392.
DR GeneID; 45425328; -.
DR KEGG; mtc:MT1392; -.
DR PATRIC; fig|83331.31.peg.1499; -.
DR HOGENOM; CLU_000604_84_9_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 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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..579
FT /note="Mycobactin import ATP-binding/permease protein IrtB"
FT /id="PRO_0000426764"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 38..52
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 74..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..146
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 147..155
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 179..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 259..579
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 17..299
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 332..567
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 366..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 579 AA; 60954 MW; 46FA562CB22AE7D8 CRC64;
MIRTWIALVP NDHRARLIGF ALLAFCSVVA RAVGTVLLVP LMAALFGEAP QRAWLWLGWL
SAATVAGWVL DAVTARIGIE LGFAVLNHTQ HDVADRLPVV RLDWFTAENT ATARQAIAAT
GPELVGLVVN LVTPLTSAIL LPAVIALALL PISWQLGVAA LAGVPLLLGA LWASAAFARR
ADTAADKANT ALTERIIEFA RTQQALRAAR RVEPARSLVG NALASQHTAT MRLLGMQIPG
QLLFSIASQL ALIVLAGTTA ALTITGTLTV PEAIALIVVM VRYLEPFTAV SELAPALEST
RATLGRIGSV LTAPVMVAGS GTWRDGAVVP RIEFDDVAFG YDGGSGPVLD GVSFCLQPGT
TTAIVGPSGC GKSTILALIA GLHQPTRGRV LIDGTDVATL DARAQQAVCS VVFQHPYLFH
GTIRDNVFAA DPGASDDQFA QAVRLARVDE LIARLPDGAN TIVGEAGSAL SGGERQRVSI
ARALLKAAPV LLVDEATSAL DAENEAAVVD ALAADPRSRT RVIVAHRLAS IRHADRVLFV
DDGRVVEDGS ISELLTAGGR FSQFWRQQHE AAEWQILAE
