ID   LPQY_MYCTU              Reviewed;         468 AA.
AC   P9WGU9; F2GFS7; L0T620; Q7ARU8; Q7D8J9;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Trehalose-binding lipoprotein LpqY;
DE   Flags: Precursor;
GN   Name=lpqY; OrderedLocusNames=Rv1235;
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, SUBUNIT, AND DISRUPTION PHENOTYPE.
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).
RN   [3]
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 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. {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:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- DISRUPTION PHENOTYPE: Mutants show no growth on trehalose as the sole
CC       carbon and energy source, but grow normally on glucose. They secrete
CC       substantial amounts of trehalose during growth on glycerol.
CC       {ECO:0000269|PubMed:21118978}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP43991.1; -; Genomic_DNA.
DR   RefSeq; NP_215751.1; NC_000962.3.
DR   RefSeq; WP_003898783.1; NZ_NVQJ01000039.1.
DR   AlphaFoldDB; P9WGU9; -.
DR   SMR; P9WGU9; -.
DR   STRING; 83332.Rv1235; -.
DR   PaxDb; P9WGU9; -.
DR   DNASU; 887145; -.
DR   GeneID; 45425205; -.
DR   GeneID; 887145; -.
DR   KEGG; mtu:Rv1235; -.
DR   PATRIC; fig|83332.111.peg.1380; -.
DR   TubercuList; Rv1235; -.
DR   eggNOG; COG1653; Bacteria.
DR   OMA; PFWANTQ; -.
DR   PhylomeDB; P9WGU9; -.
DR   BioCyc; MetaCyc:G185E-5406-MON; -.
DR   Proteomes; UP000001584; Chromosome.
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:0015771; P:trehalose transport; IDA:MTBBASE.
DR   InterPro; IPR006059; SBP.
DR   Pfam; PF01547; SBP_bac_1; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW   Signal; Sugar transport; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           26..468
FT                   /note="Trehalose-binding lipoprotein LpqY"
FT                   /id="PRO_0000419317"
FT   LIPID           26
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           26
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   468 AA;  49793 MW;  D2F5A20A706680CA CRC64;
     MVMSRGRIPR LGAAVLVALT TAAAACGADS QGLVVSFYTP ATDGATFTAI AQRCNQQFGG
     RFTIAQVSLP RSPNEQRLQL ARRLTGNDRT LDVMALDVVW TAEFAEAGWA LPLSDDPAGL
     AENDAVADTL PGPLATAGWN HKLYAAPVTT NTQLLWYRPD LVNSPPTDWN AMIAEAARLH
     AAGEPSWIAV QANQGEGLVV WFNTLLVSAG GSVLSEDGRH VTLTDTPAHR AATVSALQIL
     KSVATTPGAD PSITRTEEGS ARLAFEQGKA ALEVNWPFVF ASMLENAVKG GVPFLPLNRI
     PQLAGSINDI GTFTPSDEQF RIAYDASQQV FGFAPYPAVA PGQPAKVTIG GLNLAVAKTT
     RHRAEAFEAV RCLRDQHNQR YVSLEGGLPA VRASLYSDPQ FQAKYPMHAI IRQQLTDAAV
     RPATPVYQAL SIRLAAVLSP ITEIDPESTA DELAAQAQKA IDGMGLLP