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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}.
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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
 
 
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