PIME_MYCTU
ID PIME_MYCTU Reviewed; 431 AA.
AC P9WN01; L0T8L9; O06557; Q7D8R1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
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=Rv1159;
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 AS A MANNOSYLTRANSFERASE, AND ROLE IN VIRULENCE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16803893; DOI=10.1074/jbc.m604214200;
RA Morita Y.S., Sena C.B., Waller R.F., Kurokawa K., Sernee M.F., Nakatani F.,
RA Haites R.E., Billman-Jacobe H., McConville M.J., Maeda Y., Kinoshita T.;
RT "PimE is a polyprenol-phosphate-mannose-dependent mannosyltransferase that
RT transfers the fifth mannose of phosphatidylinositol mannoside in
RT mycobacteria.";
RL J. Biol. Chem. 281:25143-25155(2006).
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: 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:0000269|PubMed:16803893}.
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}.
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DR EMBL; AL123456; CCP43914.1; -; Genomic_DNA.
DR PIR; H70555; H70555.
DR RefSeq; NP_215675.1; NC_000962.3.
DR RefSeq; WP_003900282.1; NZ_NVQJ01000025.1.
DR AlphaFoldDB; P9WN01; -.
DR STRING; 83332.Rv1159; -.
DR PaxDb; P9WN01; -.
DR GeneID; 885899; -.
DR KEGG; mtu:Rv1159; -.
DR TubercuList; Rv1159; -.
DR eggNOG; COG1051; Bacteria.
DR OMA; TRWWLSG; -.
DR PhylomeDB; P9WN01; -.
DR BioCyc; MetaCyc:G185E-5327-MON; -.
DR UniPathway; UPA00949; -.
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:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043750; F:phosphatidylinositol alpha-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..431
FT /note="Polyprenol-phosphate-mannose-dependent alpha-(1-2)-
FT phosphatidylinositol pentamannoside mannosyltransferase"
FT /id="PRO_0000393738"
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
