PIMG_MYCS2
ID PIMG_MYCS2 Reviewed; 440 AA.
AC A0R036; I7GD51;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Polyprenol-phosphate-mannose-dependent alpha-(1-2)-phosphatidylinositol mannoside mannosyltransferase;
DE EC=2.4.1.-;
DE AltName: Full=Alpha-D-mannose-alpha-(1-2)-mannosyltransferase;
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 OrderedLocusNames=MSMEG_4247, MSMEI_4147;
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 IN LAM BIOSYNTHESIS.
RX PubMed=16945913; DOI=10.1073/pnas.0603049103;
RA Kaur D., Berg S., Dinadayala P., Gicquel B., Chatterjee D., McNeil M.R.,
RA Vissa V.D., Crick D.C., Jackson M., Brennan P.J.;
RT "Biosynthesis of mycobacterial lipoarabinomannan: role of a branching
RT mannosyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13664-13669(2006).
CC -!- FUNCTION: Responsible for the addition of alpha-(1-2) mannose branches
CC to the linear mannan core on the biosynthetic pathway to mature
CC Lipoarabinomannan (LAM). {ECO:0000269|PubMed:16945913}.
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=AFP40604.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK71149.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40604.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_888524.1; NC_008596.1.
DR AlphaFoldDB; A0R036; -.
DR STRING; 246196.MSMEI_4147; -.
DR CAZy; GT87; Glycosyltransferase Family 87.
DR PRIDE; A0R036; -.
DR EnsemblBacteria; ABK71149; ABK71149; MSMEG_4247.
DR EnsemblBacteria; AFP40604; AFP40604; MSMEI_4147.
DR KEGG; msg:MSMEI_4147; -.
DR KEGG; msm:MSMEG_4247; -.
DR PATRIC; fig|246196.19.peg.4167; -.
DR eggNOG; COG5650; Bacteria.
DR OMA; TVWAMRR; -.
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: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 1: Evidence at protein level;
KW Cell membrane; Glycosyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..440
FT /note="Polyprenol-phosphate-mannose-dependent alpha-(1-2)-
FT phosphatidylinositol mannoside mannosyltransferase"
FT /id="PRO_0000393741"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 419..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 48240 MW; 90E76D5C0A0411B8 CRC64;
MLEMSKRQSP RGAGLAPTIA WRVFQLLTLA GVLWVGWRLL GRVPYRIDID VYRMGGRAWL
DGRPLYADGA IFHTQGGLDL PFTYPPLAAI AFAPFAWLSL PLASSAITAT TLVLLIVATT
IVLTRLDVWP HTTVTSEPAW MRRAWLAAAM VAPAVIYLEP IRSNFEFGQI NVVLMTLVIA
DCVPRRTPWP RGLLLGLAIA LKLTPAVFLL YFLLRRDIHT LLRTAATAVV ASLAGFALAW
SDSVEYWTET VRNTDRIGTA TLNTNQNIAG ALARLGLGES PRFILWVLAC FAVLALTVWA
ARRALRGDTA DQTTEAPVLA LVCVALFGLV VSPVSWSHHW VWMLPVLVVT AVLAYRRRSV
WFTALTAAGL ALTVWTPITL LPEHRETTAS LWRQLAGGSY VWWAFAVIVV IGLVSSSRTH
TGDAHETDEP LVPLARGEAG
