PIME_MYCS2
ID PIME_MYCS2 Reviewed; 410 AA.
AC A0R2K8; I7G6Y4;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 82.
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=MSMEG_5149, MSMEI_5018;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION AS A MANNOSYLTRANSFERASE, MUTAGENESIS OF ASP-58; ASP-67; ASP-70;
RP ASP-77; ASP-82 AND ASP-86, NOMENCLATURE, AND ROLE IN VIRULENCE.
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).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK75499.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AFP41462.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK75499.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP41462.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_889396.1; NC_008596.1.
DR AlphaFoldDB; A0R2K8; -.
DR STRING; 246196.MSMEI_5018; -.
DR CAZy; GT87; Glycosyltransferase Family 87.
DR TCDB; 9.B.142.17.7; the integral membrane glycosyltransferase family 39 (gt39) family.
DR PRIDE; A0R2K8; -.
DR EnsemblBacteria; ABK75499; ABK75499; MSMEG_5149.
DR EnsemblBacteria; AFP41462; AFP41462; MSMEI_5018.
DR KEGG; msg:MSMEI_5018; -.
DR KEGG; msm:MSMEG_5149; -.
DR PATRIC; fig|246196.19.peg.5025; -.
DR eggNOG; COG1051; Bacteria.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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..410
FT /note="Polyprenol-phosphate-mannose-dependent alpha-(1-2)-
FT phosphatidylinositol pentamannoside mannosyltransferase"
FT /id="PRO_0000393739"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 58
FT /note="D->A: Loss of mannosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:16803893"
FT MUTAGEN 67
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16803893"
FT MUTAGEN 70
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16803893"
FT MUTAGEN 77
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16803893"
FT MUTAGEN 82
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16803893"
FT MUTAGEN 86
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16803893"
SQ SEQUENCE 410 AA; 44400 MW; 83917F5E06063A2A CRC64;
MRVNGYRGAK VGAVDTTSPP EVPASARLQR LAPMLLVVSI LARLAWTYLV PNGANFVDLH
VYVGGADALD GPGALYDYVY ADQTPDFPLP FTYPPFAAIV FYPLHLLPFG VVAFIWQIGI
IAALYGVVRV SQRLMGLQSQ RRVAMLWTAL GIWTEPLRST FDYGQVNVVL VLAVLCAVST
TRWWLSGLLV GLAAGIKLTP AVAGLYFLGA RRWAAVACSA AVFFATVGVS WLVVGAQARR
YFTELLGDAD RIGPIGTSFN QSWRGGISRI LGHDAGFGPL VLIGIGITAV LALLAWRAIG
GAQDRLGGIL VVSLFGLVLS PISWTHHWVW LIPLMMWLLH GPLSALRGAR ILGWGWLALT
LLGVPWLLSF AQPTIWEIGR PWYLAWAGLV YIVATLATLG WIAFSRKGSG
