IRTB_MYCTU
ID IRTB_MYCTU Reviewed; 579 AA.
AC P9WQJ7; 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 52.
DE RecName: Full=Mycobactin import ATP-binding/permease protein IrtB;
DE EC=7.2.2.-;
DE AltName: Full=Iron-regulated transporter B;
GN Name=irtB; OrderedLocusNames=Rv1349; ORFNames=MTCY02B10.13;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12065475; DOI=10.1128/iai.70.7.3371-3381.2002;
RA Rodriguez G.M., Voskuil M.I., Gold B., Schoolnik G.K., Smith I.;
RT "IdeR, an essential gene in Mycobacterium tuberculosis: role of IdeR in
RT iron-dependent gene expression, iron metabolism, and oxidative stress
RT response.";
RL Infect. Immun. 70:3371-3381(2002).
RN [3]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16385031; DOI=10.1128/jb.188.2.424-430.2006;
RA Rodriguez G.M., Smith I.;
RT "Identification of an ABC transporter required for iron acquisition and
RT virulence in Mycobacterium tuberculosis.";
RL J. Bacteriol. 188:424-430(2006).
RN [4]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18461140; DOI=10.1371/journal.pone.0002087;
RA Farhana A., Kumar S., Rathore S.S., Ghosh P.C., Ehtesham N.Z., Tyagi A.K.,
RA Hasnain S.E.;
RT "Mechanistic insights into a novel exporter-importer system of
RT Mycobacterium tuberculosis unravel its role in trafficking of iron.";
RL PLoS ONE 3:E2087-E2087(2008).
RN [5]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19948799; DOI=10.1128/jb.00223-09;
RA Ryndak M.B., Wang S., Smith I., Rodriguez G.M.;
RT "The Mycobacterium tuberculosis high-affinity iron importer, IrtA, contains
RT an FAD-binding domain.";
RL J. Bacteriol. 192:861-869(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:16385031, PubMed:19948799) (By similarity). Transmembrane
CC domains (TMD) form a pore in the membrane and the ATP-binding domain
CC (NBD) is responsible for energy generation (By similarity). Required
CC for replication in human macrophages and in mouse lungs
CC (PubMed:16385031). {ECO:0000250|UniProtKB:G7CBF6,
CC ECO:0000269|PubMed:16385031, ECO:0000269|PubMed:19948799}.
CC -!- SUBUNIT: Forms a heterodimer with IrtA. {ECO:0000305|PubMed:16385031,
CC ECO:0000305|PubMed:19948799}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:18461140}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:18461140}.
CC -!- INDUCTION: Repressed by iron and IdeR. {ECO:0000269|PubMed:12065475,
CC ECO:0000269|PubMed:18461140}.
CC -!- DOMAIN: In IrtB the ATP-binding domain (NBD) and the transmembrane
CC domain (TMD) are fused.
CC -!- DISRUPTION PHENOTYPE: Mutants show normal growth in iron-sufficient
CC conditions, but show a growth defect under iron-deficient conditions.
CC {ECO:0000269|PubMed:16385031}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Siderophore-
CC Fe(3+) uptake transporter (SIUT) (TC 3.A.1.21) family. {ECO:0000305}.
CC -!- CAUTION: PubMed:18461140 reports that IrtB forms a siderophore importer
CC with Rv2895c, however this activity could be due to functional
CC differences of IrtB in the molecular context of M.smegmatis and
CC M.tuberculosis. {ECO:0000305}.
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DR EMBL; AL123456; CCP44107.1; -; Genomic_DNA.
DR PIR; D70740; D70740.
DR RefSeq; NP_215865.1; NC_000962.3.
DR RefSeq; WP_003900322.1; NZ_NVQJ01000031.1.
DR AlphaFoldDB; P9WQJ7; -.
DR SMR; P9WQJ7; -.
DR STRING; 83332.Rv1349; -.
DR PaxDb; P9WQJ7; -.
DR DNASU; 886834; -.
DR GeneID; 45425328; -.
DR GeneID; 886834; -.
DR KEGG; mtu:Rv1349; -.
DR TubercuList; Rv1349; -.
DR eggNOG; COG1132; Bacteria.
DR OMA; MQVPGQL; -.
DR PhylomeDB; P9WQJ7; -.
DR Reactome; R-HSA-1222449; Mtb iron assimilation by chelation.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015343; F:siderophore transmembrane transporter activity; IDA:MTBBASE.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IEP:MTBBASE.
DR GO; GO:0044847; P:iron acquisition from host; IMP:MTBBASE.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:MTBBASE.
DR GO; GO:0075139; P:response to host iron concentration; IMP:MTBBASE.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IDA:GO_Central.
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 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_0000093257"
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..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 137..158
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 180..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..260
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 282..579
FT /note="Cytoplasmic"
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
