IRTB_MYCS2
ID IRTB_MYCS2 Reviewed; 576 AA.
AC A0R6H7; I7GB23;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 OrderedLocusNames=MSMEG_6553 {ECO:0000312|EMBL:ABK71448.1},
GN MSMEI_6376 {ECO:0000312|EMBL:AFP42802.1};
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, AND DOMAIN.
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). 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 -!- SUBUNIT: Forms a heterodimer with IrtA. {ECO:0000269|PubMed:32296173}.
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: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}.
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; CP000480; ABK71448.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42802.1; -; Genomic_DNA.
DR RefSeq; WP_011731354.1; NZ_SIJM01000033.1.
DR RefSeq; YP_890765.1; NC_008596.1.
DR AlphaFoldDB; A0R6H7; -.
DR SMR; A0R6H7; -.
DR STRING; 246196.MSMEI_6376; -.
DR PRIDE; A0R6H7; -.
DR EnsemblBacteria; ABK71448; ABK71448; MSMEG_6553.
DR EnsemblBacteria; AFP42802; AFP42802; MSMEI_6376.
DR GeneID; 66737820; -.
DR KEGG; msg:MSMEI_6376; -.
DR KEGG; msm:MSMEG_6553; -.
DR PATRIC; fig|246196.19.peg.6377; -.
DR eggNOG; COG1132; Bacteria.
DR OMA; MQVPGQL; -.
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 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..576
FT /note="Mycobactin import ATP-binding/permease protein IrtB"
FT /id="PRO_0000450630"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 47..52
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 74..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 174..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 263..267
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 289..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 19..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 576 AA; 60650 MW; C2EE429B8F8A10C3 CRC64;
MIRTLIALVP ADKRGTLGLY TVLTVLSVVI RAAGTVLLVP LVAALFGDTP QDAWPWLGWL
TAATAAGWIV DTTTSRLGFD LGFAVLDHTQ HDVADRMPNI RLDWLTAENT ATARAAIAST
GPELVGLVVN LLTPLIGAVL LPAAIAVALV AVSPPLGLAA LAGVVVLLGA MWASNRLSRK
ADTVADETNS AFTERIIEFA RTQQALRAAR RVEPARSLVG DALGAQHGAG VRLLAMQIPG
QLLFSLASQL ALILLAGMAT WLTVRGELSV PEAVAMIVVV ARYLEPFTSL SELTPAIEST
RGTLGRIRAV LDAPTLTAGD AAPADTKSAP RIEFDCVTFG YGDHPVLDDV SFVLEPGSTT
AIVGPSGSGK STILSLIAGL HQPTEGRVLI DGVDAASLDD ESRRAATSVV FQQPYLFDGS
IRDNILVGDP GADEDRLAAA VRLARVDELT ARLPNGDASK VGEAGAALSG GERQRVSIAR
ALVKPAPVLL VDEATSALDT ENEAAVVDAL TADLRHRTRV IVAHRLASIR HADRVLFLDG
GRIVEDGTID GLLAAGGRFD EFWRRQHEAA DWQITH