PPMNT_MYCTU
ID PPMNT_MYCTU Reviewed; 874 AA.
AC O53493; F2GDY6; I6Y888; L0TBC5;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase;
DE Includes:
DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000303|PubMed:19661058};
DE Short=ALP N-acyltransferase {ECO:0000250|UniProtKB:P23930};
DE EC=2.3.1.269 {ECO:0000269|PubMed:12427759};
DE Includes:
DE RecName: Full=Polyprenol monophosphomannose synthase {ECO:0000303|PubMed:11931640};
DE Short=PPM synthase {ECO:0000303|PubMed:11931640};
DE Short=Polyprenol-P-Man synthase {ECO:0000303|PubMed:12427759};
DE Short=Ppm1 {ECO:0000303|PubMed:11931640};
DE EC=2.4.1.- {ECO:0000269|PubMed:11931640};
DE AltName: Full=Dolichol-phosphate mannose synthase;
DE EC=2.4.1.83 {ECO:0000269|PubMed:11931640};
GN Name=ppm1 {ECO:0000303|PubMed:11931640};
GN Synonyms=lnt {ECO:0000305|PubMed:19661058}; OrderedLocusNames=Rv2051c;
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 PHOSPHOMANNOSE SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, DOMAIN, AND EXPRESSION IN M.SMEGMATIS.
RX PubMed=11931640; DOI=10.1042/bj20020107;
RA Gurcha S.S., Baulard A.R., Kremer L., Locht C., Moody D.B., Muhlecker W.,
RA Costello C.E., Crick D.C., Brennan P.J., Besra G.S.;
RT "Ppm1, a novel polyprenol monophosphomannose synthase from Mycobacterium
RT tuberculosis.";
RL Biochem. J. 365:441-450(2002).
RN [3]
RP SUBCELLULAR LOCATION, DOMAIN, AND TOPOLOGY.
RX PubMed=12427759; DOI=10.1074/jbc.m207922200;
RA Baulard A.R., Gurcha S.S., Engohang-Ndong J., Gouffi K., Locht C.,
RA Besra G.S.;
RT "In vivo interaction between the polyprenol phosphate mannose synthase Ppm1
RT and the integral membrane protein Ppm2 from Mycobacterium smegmatis
RT revealed by a bacterial two-hybrid system.";
RL J. Biol. Chem. 278:2242-2248(2003).
RN [4]
RP FUNCTION AS AN N-ACYLTRANSFERASE.
RX PubMed=19661058; DOI=10.1074/jbc.m109.022715;
RA Tschumi A., Nai C., Auchli Y., Hunziker P., Gehrig P., Keller P., Grau T.,
RA Sander P.;
RT "Identification of apolipoprotein N-acyltransferase (Lnt) in
RT mycobacteria.";
RL J. Biol. Chem. 284:27146-27156(2009).
RN [5]
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 phospholipid dependent N-acylation of the N-
CC terminal cysteine of apolipoprotein, the last step in lipoprotein
CC maturation. {ECO:0000269|PubMed:19661058}.
CC -!- FUNCTION: Transfers mannose from GDP-mannose to lipid acceptors (works
CC best on C20-C95 lipid monophosphate substrates in which the lipid can
CC be modified, tested with the C-terminal domain expressed in
CC M.smegmatis) to form polyprenol monophosphomannose (PPM). PMM is an
CC alkai-stable sugar donor which adds mannose-phosphate residues to
CC triacylated-phosphatidyl-myo-inositol mannosides (PIM2), eventually
CC leading to generation of the cell wall glycolipid lipoglycan modulins
CC lipoarabinomannan (LAM) and lipomannan (LM).
CC {ECO:0000269|PubMed:11931640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-
CC cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) +
CC N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein];
CC Xref=Rhea:RHEA:48228, Rhea:RHEA-COMP:14681, Rhea:RHEA-COMP:14684,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136912, ChEBI:CHEBI:140656,
CC ChEBI:CHEBI:140657, ChEBI:CHEBI:140660; EC=2.3.1.269;
CC Evidence={ECO:0000269|PubMed:19661058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-
CC D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83;
CC Evidence={ECO:0000269|PubMed:11931640};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC transfer).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12427759};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: Consists of 2 domains; the N-terminus (residues 1-593) probably
CC has the N-acyltransferase activity while the C-terminus (residues 594-
CC 874) has polyprenol monophosphomannose (PPM) synthase activity. The
CC whole protein has higher PPM synthase than the second domain alone when
CC expressed in M.smegmatis, suggesting the N-acyltransferase domain plays
CC a stimulating role in PPM synthesis. {ECO:0000269|PubMed:11931640,
CC ECO:0000269|PubMed:12427759}.
CC -!- MISCELLANEOUS: In a number of other Mycobacteria, including M.avis,
CC M.leprae and M.smegmatis, these domains are encoded by 2 separate
CC adjacent genes. {ECO:0000305|PubMed:11931640}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CN hydrolase
CC family. Apolipoprotein N-acyltransferase subfamily.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44824.1; -; Genomic_DNA.
DR RefSeq; NP_216567.1; NC_000962.3.
DR RefSeq; WP_003902238.1; NZ_NVQJ01000047.1.
DR AlphaFoldDB; O53493; -.
DR SMR; O53493; -.
DR STRING; 83332.Rv2051c; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; O53493; -.
DR PRIDE; O53493; -.
DR GeneID; 887402; -.
DR KEGG; mtu:Rv2051c; -.
DR PATRIC; fig|83332.111.peg.2287; -.
DR TubercuList; Rv2051c; -.
DR eggNOG; COG0463; Bacteria.
DR eggNOG; COG0815; Bacteria.
DR OMA; ADEMPND; -.
DR PhylomeDB; O53493; -.
DR BioCyc; MetaCyc:G185E-6255-MON; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0052553; P:modulation by symbiont of host immune response; IDA:MTBBASE.
DR CDD; cd07571; ALP_N-acyl_transferase; 1.
DR CDD; cd06442; DPM1_like; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_01148; Lnt; 1.
DR InterPro; IPR004563; Apolipo_AcylTrfase.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR039528; DPM1-like.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR045378; LNT_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43398; PTHR43398; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF20154; LNT_N; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00546; lnt; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell membrane; Glycosyltransferase; Hydrolase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..874
FT /note="Bifunctional apolipoprotein N-
FT acyltransferase/polyprenol monophosphomannose synthase"
FT /id="PRO_0000434582"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TRANSMEM 23..42
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TOPO_DOM 43..71
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TRANSMEM 72..89
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TOPO_DOM 90..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TOPO_DOM 116..176
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TRANSMEM 177..194
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TOPO_DOM 195..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TRANSMEM 206..223
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TOPO_DOM 224..508
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:12427759"
FT TRANSMEM 509..526
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A0QZ13"
FT TOPO_DOM 527..874
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12427759"
FT DOMAIN 241..497
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 1..593
FT /note="Apolipoprotein N-acyltransferase"
FT REGION 533..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..874
FT /note="Polyprenol monophosphomannose synthase"
FT /evidence="ECO:0000269|PubMed:11931640"
FT REGION 852..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 409
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 874 AA; 93824 MW; E00EADD2EC3238B4 CRC64;
MKLGAWVAAQ LPTTRTAVRT RLTRLVVSIV AGLLLYASFP PRNCWWAAVV ALALLAWVLT
HRATTPVGGL GYGLLFGLVF YVSLLPWIGE LVGPGPWLAL ATTCALFPGI FGLFAVVVRL
LPGWPIWFAV GWAAQEWLKS ILPFGGFPWG SVAFGQAEGP LLPLVQLGGV ALLSTGVALV
GCGLTAIALE IEKWWRTGGQ GDAPPAVVLP AACICLVLFA AIVVWPQVRH AGSGSGGEPT
VTVAVVQGNV PRLGLDFNAQ RRAVLDNHVE ETLRLAADVH AGLAQQPQFV IWPENSSDID
PFVNPDAGQR ISAAAEAIGA PILIGTLMDV PGRPRENPEW TNTAIVWNPG TGPADRHDKA
IVQPFGEYLP MPWLFRHLSG YADRAGHFVP GNGTGVVRIA GVPVGVATCW EVIFDRAPRK
SILGGAQLLT VPSNNATFNK TMSEQQLAFA KVRAVEHDRY VVVAGTTGIS AVIAPDGGEL
IRTDFFQPAY LDSQVRLKTR LTPATRWGPI LQWILVGAAA AVVLVAMRQN GWFPRPRRSE
PKGENDDSDA PPGRSEASGP PALSESDDEL IQPEQGGRHS SGFGRHRATS RSYMTTGQPA
PPAPGNRPSQ RVLVIIPTFN ERENLPVIHR RLTQACPAVH VLVVDDSSPD GTGQLADELA
QADPGRTHVM HRTAKNGLGA AYLAGFAWGL SREYSVLVEM DADGSHAPEQ LQRLLDAVDA
GADLAIGSRY VAGGTVRNWP WRRLVLSKTA NTYSRLALGI GIHDITAGYR AYRREALEAI
DLDGVDSKGY CFQIDLTWRT VSNGFVVTEV PITFTERELG VSKMSGSNIR EALVKVARWG
IEGRLSRSDH ARARPDIARP GAGGSRVSRA DVTE
