ID   PIME_MYCTO              Reviewed;         431 AA.
AC   P9WN00; L0T8L9; O06557; Q7D8R1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Polyprenol-phosphate-mannose-dependent alpha-(1-2)-phosphatidylinositol pentamannoside mannosyltransferase;
DE            EC=2.4.1.-;
DE   AltName: Full=Alpha-mannosyltransferase;
DE            Short=Alpha-ManT;
DE   AltName: Full=PPM-dependent mannosyltransferase;
DE   AltName: Full=Polyprenol-phosphate-mannose alpha-mannosyltransferase;
DE            Short=PPM alpha-mannosyltransferase;
GN   Name=pimE; OrderedLocusNames=MT1195;
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: Catalyzes the alpha-1,2 addition of a mannose residue from
CC       polyprenol-phosphate-mannose (PPM) to a monoacyl phosphatidylinositol
CC       pentamannoside (AcPIM5) to generate a monoacyl phosphatidylinositol
CC       hexamannoside (AcPIM6). {ECO:0000250}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 87 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45452.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45452.1; ALT_INIT; Genomic_DNA.
DR   PIR; H70555; H70555.
DR   RefSeq; WP_003900282.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WN00; -.
DR   CAZy; GT87; Glycosyltransferase Family 87.
DR   EnsemblBacteria; AAK45452; AAK45452; MT1195.
DR   KEGG; mtc:MT1195; -.
DR   PATRIC; fig|83331.31.peg.1295; -.
DR   HOGENOM; CLU_034641_1_0_11; -.
DR   UniPathway; UPA00949; -.
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:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR018584; GT87.
DR   Pfam; PF09594; GT87; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW   Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..431
FT                   /note="Polyprenol-phosphate-mannose-dependent alpha-(1-2)-
FT                   phosphatidylinositol pentamannoside mannosyltransferase"
FT                   /id="PRO_0000427213"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   431 AA;  47102 MW;  CB24BD99489D2896 CRC64;
     MCRTLIDGPV RSAIAKVRQI DTTSSTPAAA RRVTSPPARE TRAAVLLLVL SVGARLAWTY
     LAPNGANFVD LHVYVSGAAS LDHPGTLYGY VYADQTPDFP LPFTYPPFAA VVFYPLHLVP
     FGLIALLWQV VTMAALYGAV RISQRLMGGT AETGHFAAML WTAIAIWIEP LRSTFDYGQI
     NVLLMLAALW AVYTPRWWLS GLLVGVASGV KLTPAITAVY LVGVRRLHAA AFSVVVFLAT
     VGVSLLVVGD EARYYFTDLL GDAGRVGPIA TSFNQSWRGA ISRILGHDAG FGPLVLAAIA
     STAVLAILAW RALDRSDRLG KLLVVELFGL LLSPISWTHH WVWLVPLMIW LIDGPARERP
     GARILGWGWL VLTIVGVPWL LSFAQPSIWQ IGRPWYLAWA GLVYVVATLA TLGWIAASER
     YVRIRPRRMA N