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Protein

Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase

Gene

ppm1

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transfers a fatty acyl group to the free alpha-amino group (N-acylation) on the N-terminus of membrane apolipoproteins.1 Publication
Transfers mannose from GDP-mannose to lipid acceptors (works best on C20-C95 lipid monophosphate substrates in which the lipid can be modified, tested with the C-terminal domain expressed in M.smegmatis) to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor which adds mannose-phosphate residues to triacylated-phosphatidyl-myo-inositol mannosides (PIM2), eventually leading to generation of the cell wall glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM).1 Publication

Catalytic activityi

GDP-mannose + polyprenol phosphate = GDP + dolichyl D-mannosyl phosphate.1 Publication
GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.1 Publication

Pathwayi: lipoprotein biosynthesis (N-acyl transfer)

This protein is involved in the pathway lipoprotein biosynthesis (N-acyl transfer), which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway lipoprotein biosynthesis (N-acyl transfer) and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Glycosyltransferase, Hydrolase, Transferase

Enzyme and pathway databases

BioCyciMTBRV:RV2051C-MONOMER.
UniPathwayiUPA00666.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase
Including the following 2 domains:
Apolipoprotein N-acyltransferase1 Publication (EC:2.3.1.-)
Polyprenol monophosphomannose synthase1 Publication (EC:2.4.1.-1 Publication)
Short name:
PPM synthase1 Publication
Short name:
Polyprenol-P-Man synthase1 Publication
Short name:
Ppm11 Publication
Alternative name(s):
Dolichol-phosphate mannose synthase (EC:2.4.1.831 Publication)
Gene namesi
Name:ppm11 Publication
Synonyms:lnt1 Publication
Ordered Locus Names:Rv2051c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2051c.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicBy similarityAdd
BLAST
Transmembranei23 – 4220HelicalBy similarityAdd
BLAST
Topological domaini43 – 7129ExtracellularBy similarityAdd
BLAST
Transmembranei72 – 8918HelicalBy similarityAdd
BLAST
Topological domaini90 – 934CytoplasmicBy similarity
Transmembranei94 – 11522HelicalBy similarityAdd
BLAST
Topological domaini116 – 17661ExtracellularBy similarityAdd
BLAST
Transmembranei177 – 19418HelicalBy similarityAdd
BLAST
Topological domaini195 – 20511CytoplasmicBy similarityAdd
BLAST
Transmembranei206 – 22318HelicalBy similarityAdd
BLAST
Topological domaini224 – 508285Extracellular1 PublicationAdd
BLAST
Transmembranei509 – 52618HelicalBy similarityAdd
BLAST
Topological domaini527 – 874348Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 874874Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthasePRO_0000434582Add
BLAST

Proteomic databases

PaxDbiO53493.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv2051c.

Structurei

3D structure databases

ProteinModelPortaliO53493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini241 – 543303CN hydrolasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 593593Apolipoprotein N-acyltransferaseAdd
BLAST
Regioni594 – 874281Polyprenol monophosphomannose synthase1 PublicationAdd
BLAST

Domaini

Consists of 2 domains; the N-terminus (residues 1-593) probably has the N-acyltransferase activity while the C-terminus (residues 594-874) has polyprenol monophosphomannose (PPM) synthase activity. The whole protein has higher PPM synthase than the second domain alone when expressed in M.smegmatis, suggesting the N-acyltransferase domain plays a stimulating role in PPM synthesis.2 Publications

Sequence similaritiesi

In the N-terminal section; belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily.
In the C-terminal section; belongs to the glycosyltransferase 2 family.Curated
Contains 1 CN hydrolase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107R05. Bacteria.
COG0815. LUCA.
HOGENOMiHOG000021324.
KOiK03820.
OMAiAGHFVPR.
OrthoDBiEOG6C8N0Z.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
3.90.550.10. 1 hit.
HAMAPiMF_01148. Lnt.
InterProiIPR004563. Apolipo_AcylTrfase.
IPR003010. C-N_Hydrolase.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
SSF56317. SSF56317. 1 hit.
TIGRFAMsiTIGR00546. lnt. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O53493-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLGAWVAAQ LPTTRTAVRT RLTRLVVSIV AGLLLYASFP PRNCWWAAVV
60 70 80 90 100
ALALLAWVLT HRATTPVGGL GYGLLFGLVF YVSLLPWIGE LVGPGPWLAL
110 120 130 140 150
ATTCALFPGI FGLFAVVVRL LPGWPIWFAV GWAAQEWLKS ILPFGGFPWG
160 170 180 190 200
SVAFGQAEGP LLPLVQLGGV ALLSTGVALV GCGLTAIALE IEKWWRTGGQ
210 220 230 240 250
GDAPPAVVLP AACICLVLFA AIVVWPQVRH AGSGSGGEPT VTVAVVQGNV
260 270 280 290 300
PRLGLDFNAQ RRAVLDNHVE ETLRLAADVH AGLAQQPQFV IWPENSSDID
310 320 330 340 350
PFVNPDAGQR ISAAAEAIGA PILIGTLMDV PGRPRENPEW TNTAIVWNPG
360 370 380 390 400
TGPADRHDKA IVQPFGEYLP MPWLFRHLSG YADRAGHFVP GNGTGVVRIA
410 420 430 440 450
GVPVGVATCW EVIFDRAPRK SILGGAQLLT VPSNNATFNK TMSEQQLAFA
460 470 480 490 500
KVRAVEHDRY VVVAGTTGIS AVIAPDGGEL IRTDFFQPAY LDSQVRLKTR
510 520 530 540 550
LTPATRWGPI LQWILVGAAA AVVLVAMRQN GWFPRPRRSE PKGENDDSDA
560 570 580 590 600
PPGRSEASGP PALSESDDEL IQPEQGGRHS SGFGRHRATS RSYMTTGQPA
610 620 630 640 650
PPAPGNRPSQ RVLVIIPTFN ERENLPVIHR RLTQACPAVH VLVVDDSSPD
660 670 680 690 700
GTGQLADELA QADPGRTHVM HRTAKNGLGA AYLAGFAWGL SREYSVLVEM
710 720 730 740 750
DADGSHAPEQ LQRLLDAVDA GADLAIGSRY VAGGTVRNWP WRRLVLSKTA
760 770 780 790 800
NTYSRLALGI GIHDITAGYR AYRREALEAI DLDGVDSKGY CFQIDLTWRT
810 820 830 840 850
VSNGFVVTEV PITFTERELG VSKMSGSNIR EALVKVARWG IEGRLSRSDH
860 870
ARARPDIARP GAGGSRVSRA DVTE
Length:874
Mass (Da):93,824
Last modified:June 1, 1998 - v1
Checksum:iE00EADD2EC3238B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44824.1.
RefSeqiNP_216567.1. NC_000962.3.
WP_003902238.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP44824; CCP44824; Rv2051c.
GeneIDi887402.
KEGGimtu:Rv2051c.
mtv:RVBD_2051c.
PATRICi18153122. VBIMycTub87468_2290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44824.1.
RefSeqiNP_216567.1. NC_000962.3.
WP_003902238.1. NC_000962.3.

3D structure databases

ProteinModelPortaliO53493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2051c.

Proteomic databases

PaxDbiO53493.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44824; CCP44824; Rv2051c.
GeneIDi887402.
KEGGimtu:Rv2051c.
mtv:RVBD_2051c.
PATRICi18153122. VBIMycTub87468_2290.

Organism-specific databases

TubercuListiRv2051c.

Phylogenomic databases

eggNOGiENOG4107R05. Bacteria.
COG0815. LUCA.
HOGENOMiHOG000021324.
KOiK03820.
OMAiAGHFVPR.
OrthoDBiEOG6C8N0Z.

Enzyme and pathway databases

UniPathwayiUPA00666.
BioCyciMTBRV:RV2051C-MONOMER.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
3.90.550.10. 1 hit.
HAMAPiMF_01148. Lnt.
InterProiIPR004563. Apolipo_AcylTrfase.
IPR003010. C-N_Hydrolase.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
SSF56317. SSF56317. 1 hit.
TIGRFAMsiTIGR00546. lnt. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "Ppm1, a novel polyprenol monophosphomannose synthase from Mycobacterium tuberculosis."
    Gurcha S.S., Baulard A.R., Kremer L., Locht C., Moody D.B., Muhlecker W., Costello C.E., Crick D.C., Brennan P.J., Besra G.S.
    Biochem. J. 365:441-450(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A PHOSPHOMANNOSE SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DOMAIN, EXPRESSION IN M.SMEGMATIS.
  3. "In vivo interaction between the polyprenol phosphate mannose synthase Ppm1 and the integral membrane protein Ppm2 from Mycobacterium smegmatis revealed by a bacterial two-hybrid system."
    Baulard A.R., Gurcha S.S., Engohang-Ndong J., Gouffi K., Locht C., Besra G.S.
    J. Biol. Chem. 278:2242-2248(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAIN, TOPOLOGY.
  4. "Identification of apolipoprotein N-acyltransferase (Lnt) in mycobacteria."
    Tschumi A., Nai C., Auchli Y., Hunziker P., Gehrig P., Keller P., Grau T., Sander P.
    J. Biol. Chem. 284:27146-27156(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN N-ACYLTRANSFERASE.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiPPMNT_MYCTU
AccessioniPrimary (citable) accession number: O53493
Secondary accession number(s): F2GDY6, I6Y888, L0TBC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 11, 2015
Last sequence update: June 1, 1998
Last modified: December 9, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In a number of other Mycobacteria, including M.avis, M.leprae and M.smegmatis, these domains are encoded by 2 separate adjacent genes.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.