ID   SUGA_MYCTU              Reviewed;         307 AA.
AC   P9WG03; F2GFS6; L0T699; O50452; Q7D8J8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Trehalose transport system permease protein SugA;
GN   Name=sugA; OrderedLocusNames=Rv1236;
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   FUNCTION IN TREHALOSE IMPORT, AND SUBUNIT.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21118978; DOI=10.1073/pnas.1014642108;
RA   Kalscheuer R., Weinrick B., Veeraraghavan U., Besra G.S., Jacobs W.R. Jr.;
RT   "Trehalose-recycling ABC transporter LpqY-SugA-SugB-SugC is essential for
RT   virulence of Mycobacterium tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:21761-21766(2010).
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. {ECO:0000269|PubMed:21118978}.
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:0000305|PubMed:21118978}.
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; AL123456; CCP43992.1; -; Genomic_DNA.
DR   PIR; C70952; C70952.
DR   RefSeq; NP_215752.1; NC_000962.3.
DR   RefSeq; WP_003406295.1; NZ_NVQJ01000039.1.
DR   AlphaFoldDB; P9WG03; -.
DR   SMR; P9WG03; -.
DR   STRING; 83332.Rv1236; -.
DR   PaxDb; P9WG03; -.
DR   DNASU; 887124; -.
DR   GeneID; 45425206; -.
DR   GeneID; 887124; -.
DR   KEGG; mtu:Rv1236; -.
DR   TubercuList; Rv1236; -.
DR   eggNOG; COG1175; Bacteria.
DR   OMA; LWYSVQS; -.
DR   PhylomeDB; P9WG03; -.
DR   BioCyc; MetaCyc:G185E-5407-MON; -.
DR   Proteomes; UP000001584; 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:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
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   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Sugar transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..307
FT                   /note="Trehalose transport system permease protein SugA"
FT                   /id="PRO_0000419315"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          85..291
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   307 AA;  33051 MW;  8B88E852E40F622D CRC64;
     MTSVEQRTAT AVFSRTGSRM AERRLAFMLV APAAMLMVAV TAYPIGYALW LSLQRNNLAT
     PNDTAFIGLG NYHTILIDRY WWTALAVTLA ITAVSVTIEF VLGLALALVM HRTLIGKGLV
     RTAVLIPYGI VTVVASYSWY YAWTPGTGYL ANLLPYDSAP LTQQIPSLGI VVIAEVWKTT
     PFMSLLLLAG LALVPEDLLR AAQVDGASAW RRLTKVILPM IKPAIVVALL FRTLDAFRIF
     DNIYVLTGGS NNTGSVSILG YDNLFKGFNV GLGSAISVLI FGCVAVIAFI FIKLFGAAAP
     GGEPSGR