PIMG_MYCTU
ID PIMG_MYCTU Reviewed; 427 AA.
AC P9WMZ9; L0TAF3; O53515; Q7D7E4;
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 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=Rv2181;
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 IN LAM BIOSYNTHESIS.
RC STRAIN=ATCC 25618 / H37Rv;
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).
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: 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}.
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DR EMBL; AL123456; CCP44958.1; -; Genomic_DNA.
DR PIR; G70936; G70936.
DR RefSeq; NP_216697.1; NC_000962.3.
DR RefSeq; WP_003411339.1; NZ_NVQJ01000008.1.
DR AlphaFoldDB; P9WMZ9; -.
DR STRING; 83332.Rv2181; -.
DR PaxDb; P9WMZ9; -.
DR GeneID; 45426157; -.
DR GeneID; 888269; -.
DR KEGG; mtu:Rv2181; -.
DR TubercuList; Rv2181; -.
DR eggNOG; COG5650; Bacteria.
DR OMA; TVWAMRR; -.
DR PhylomeDB; P9WMZ9; -.
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:0000026; F:alpha-1,2-mannosyltransferase activity; IMP:MTBBASE.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IMP:MTBBASE.
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..427
FT /note="Polyprenol-phosphate-mannose-dependent alpha-(1-2)-
FT phosphatidylinositol mannoside mannosyltransferase"
FT /id="PRO_0000393740"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 427 AA; 47143 MW; C5B1A18175A661CE CRC64;
MSAWRAPEVG SRLGRRVLWC LLWLLAGVAL GYVAWRLFGH TPYRIDIDIY QMGARAWLDG
RPLYGGGVLF HTPIGLNLPF TYPPLAAVLF SPFAWLQMPA ASVAITVLTL VLLIASTAIV
LTGLDAWPTS RLVPAPARLR RLWLAVLIVA PATIWLEPIS SNFAFGQINV VLMTLVIVDC
FPRRTPWPRG LMLGLGIALK LTPAVFLLYF LLRRDGRAAL TALASFAVAT LLGFVLAWRD
SWEYWTHTLH HTDRIGAAAL NTDQNIAGAL ARLTIGDDER FALWVAGSLL VLAATIWAMR
RVLRAGEPTL AVICVALFGL VVSPVSWSHH WVWMLPAVLV IGLLGWRRRN VALAMLSLAG
VVLMRWTPID LLPQHRETTA VWWRQLAGMS YVWWALAVIV VAGLTVTARM TPQRSLTRGL
TPAPTAS
