LPQW_MYCTO
ID LPQW_MYCTO Reviewed; 635 AA.
AC P9WGU6; 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 38.
DE RecName: Full=Probable monoacyl phosphatidylinositol tetramannoside-binding protein LpqW;
DE Flags: Precursor;
GN Name=lpqW; OrderedLocusNames=MT1203;
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: 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}.
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DR EMBL; AE000516; AAK45460.1; -; Genomic_DNA.
DR PIR; F70874; F70874.
DR RefSeq; WP_003406102.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGU6; -.
DR SMR; P9WGU6; -.
DR EnsemblBacteria; AAK45460; AAK45460; MT1203.
DR GeneID; 45425138; -.
DR KEGG; mtc:MT1203; -.
DR PATRIC; fig|83331.31.peg.1303; -.
DR HOGENOM; CLU_027950_0_0_11; -.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000001020; Chromosome.
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 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW Phospholipid metabolism; 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_0000428300"
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