ID   LPQW_MYCTU              Reviewed;         635 AA.
AC   P9WGU7; L0T633; O50422; Q7D8Q4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Probable monoacyl phosphatidylinositol tetramannoside-binding protein LpqW;
DE   Flags: Precursor;
GN   Name=lpqW; OrderedLocusNames=Rv1166;
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   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: May directly or indirectly regulate the accessibility of the
CC       key branch point intermediate, monoacyl phosphatidylinositol
CC       tetramannoside (AcPIM4), to the elongating alpha-1,6
CC       mannosyltransferases which could regulate the lipoarabinomannans (LAMs)
CC       biosynthesis. {ECO:0000250}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {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; AL123456; CCP43922.1; -; Genomic_DNA.
DR   PIR; F70874; F70874.
DR   RefSeq; NP_215682.1; NC_000962.3.
DR   RefSeq; WP_003406102.1; NZ_NVQJ01000025.1.
DR   AlphaFoldDB; P9WGU7; -.
DR   SMR; P9WGU7; -.
DR   STRING; 83332.Rv1166; -.
DR   PaxDb; P9WGU7; -.
DR   DNASU; 886036; -.
DR   GeneID; 45425138; -.
DR   GeneID; 886036; -.
DR   KEGG; mtu:Rv1166; -.
DR   TubercuList; Rv1166; -.
DR   eggNOG; COG0747; Bacteria.
DR   OMA; TPRVMQL; -.
DR   UniPathway; UPA00949; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IMP:MTBBASE.
DR   GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR039424; SBP_5.
DR   InterPro; IPR000914; SBP_5_dom.
DR   PANTHER; PTHR30290; PTHR30290; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
PE   1: Evidence at protein level;
KW   Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Signal; Virulence.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..635
FT                   /note="Probable monoacyl phosphatidylinositol
FT                   tetramannoside-binding protein LpqW"
FT                   /id="PRO_0000393727"
FT   REGION          32..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..52
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..542
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   635 AA;  66130 MW;  216DDABF33025F1F CRC64;
     MGVPSPVRRV CVTVGALVAL ACMVLAGCTV SPPPAPQSTD TPRSTPPPPR RPTQIIMGID
     WIGPGFNPHL LSDLSPVNAA ISALVLPSAF RPIPDPNTPT GSRWEMDPTL LVSADVTNNH
     PFTVTYKIRP EAQWTDNAPI AADDFWYLWQ QMVTQPGVVD PAGYHLITSV QSLEGGKQAV
     VTFAQPYPAW RELFTDILPA HIVKDIPGGF ASGLARALPV TGGQFRVENI DPQRDEILIA
     RNDRYWGPPS KPGIILFRRA GAPAALADSV RNGDTQVAQV HGGSAAFAQL SAIPDVRTAR
     IVTPRVMQFT LRANVPKLAD TQVRKAILGL LDVDLLAAVG AGTDNTVTLD QAQIRSPSDP
     GYVPTAPPAM SSAAALGLLE ASGFQVDTNT SVSPAPSVPD STTTSVSTGP PEVIRGRISK
     DGEQLTLVIG VAANDPTSVA VANTAADQLR DVGIAATVLA LDPVTLYHDA LNDNRVDAIV
     GWRQAGGNLA TLLASRYGCP ALQATTVPAA NAPTTAPSAP IGPTPSAAPD TATPPPTAPR
     RPSDPGALVK APSNLTGICD RSIQSNIDAA LNGTKNINDV ITAVEPRLWN MSTVLPILQD
     TTIVAAGPSV QNVSLSGAVP VGIVGDAGQW VKTGQ