SUGB_MYCTO
ID SUGB_MYCTO Reviewed; 274 AA.
AC P9WG00; F2GFS5; L0T918; O50453; Q7D8J7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Trehalose transport system permease protein SugB;
GN Name=sugB; OrderedLocusNames=MT1275;
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 LpqY-SugA-SugB-SugC,
CC which is highly specific for uptake of trehalose. Involved in the
CC recycling of extracellular trehalose released from trehalose-containing
CC molecules synthesized by M.tuberculosis. Trehalose uptake is essential
CC for virulence. Probably responsible for the translocation of the
CC substrate across the membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (SugC),
CC two transmembrane proteins (Suga and SugB) and a solute-binding protein
CC (LpqY). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; AE000516; AAK45533.1; -; Genomic_DNA.
DR PIR; D70952; D70952.
DR RefSeq; WP_003900298.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WG00; -.
DR SMR; P9WG00; -.
DR EnsemblBacteria; AAK45533; AAK45533; MT1275.
DR GeneID; 45425207; -.
DR KEGG; mtc:MT1275; -.
DR PATRIC; fig|83331.31.peg.1378; -.
DR HOGENOM; CLU_016047_1_2_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:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..274
FT /note="Trehalose transport system permease protein SugB"
FT /id="PRO_0000428448"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 66..259
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 274 AA; 29158 MW; 772A9A53F559332C CRC64;
MGARRATYWA VLDTLVVGYA LLPVLWIFSL SLKPTSTVKD GKLIPSTVTF DNYRGIFRGD
LFSSALINSI GIGLITTVIA VVLGAMAAYA VARLEFPGKR LLIGAALLIT MFPSISLVTP
LFNIERAIGL FDTWPGLILP YITFALPLAI YTLSAFFREI PWDLEKAAKM DGATPGQAFR
KVIVPLAAPG LVTAAILVFI FAWNDLLLAL SLTATKAAIT APVAIANFTG SSQFEEPTGS
IAAGAIVITI PIIVFVLIFQ RRIVAGLTSG AVKG