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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: -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

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

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei294Proton acceptorPROSITE-ProRule annotation1
Active sitei359PROSITE-ProRule annotation1
Active sitei409NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • glycolipid biosynthetic process Source: MTBBASE
  • lipoprotein biosynthetic process Source: InterPro
  • modulation by symbiont of host immune response Source: MTBBASE

Keywordsi

Molecular functionAcyltransferase, Glycosyltransferase, Hydrolase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:G185E-6255-MONOMER
UniPathwayiUPA00666

Protein family/group databases

CAZyiGT2 Glycosyltransferase Family 2

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)DescriptionActionsGraphical viewLength
Topological domaini1 – 22CytoplasmicBy similarityAdd BLAST22
Transmembranei23 – 42HelicalBy similarityAdd BLAST20
Topological domaini43 – 71ExtracellularBy similarityAdd BLAST29
Transmembranei72 – 89HelicalBy similarityAdd BLAST18
Topological domaini90 – 93CytoplasmicBy similarity4
Transmembranei94 – 115HelicalBy similarityAdd BLAST22
Topological domaini116 – 176ExtracellularBy similarityAdd BLAST61
Transmembranei177 – 194HelicalBy similarityAdd BLAST18
Topological domaini195 – 205CytoplasmicBy similarityAdd BLAST11
Transmembranei206 – 223HelicalBy similarityAdd BLAST18
Topological domaini224 – 508Extracellular1 PublicationAdd BLAST285
Transmembranei509 – 526HelicalBy similarityAdd BLAST18
Topological domaini527 – 874Cytoplasmic1 PublicationAdd BLAST348

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MTBBASE

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004345821 – 874Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthaseAdd BLAST874

Proteomic databases

PaxDbiO53493
PRIDEiO53493

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv2051c

Structurei

3D structure databases

ProteinModelPortaliO53493
SMRiO53493
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini241 – 497CN hydrolasePROSITE-ProRule annotationAdd BLAST257

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 593Apolipoprotein N-acyltransferaseAdd BLAST593
Regioni594 – 874Polyprenol monophosphomannose synthase1 PublicationAdd BLAST281

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107R05 Bacteria
COG0815 LUCA
HOGENOMiHOG000021324
KOiK03820
OMAiADEMPND

Family and domain databases

CDDicd07571 ALP_N-acyl_transferase, 1 hit
Gene3Di3.60.110.10, 1 hit
3.90.550.10, 1 hit
HAMAPiMF_01148 Lnt, 1 hit
InterProiView protein in InterPro
IPR004563 Apolipo_AcylTrfase
IPR003010 C-N_Hydrolase
IPR036526 C-N_Hydrolase_sf
IPR001173 Glyco_trans_2-like
IPR029044 Nucleotide-diphossugar_trans
PfamiView protein in Pfam
PF00795 CN_hydrolase, 1 hit
PF00535 Glycos_transf_2, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit
SSF56317 SSF56317, 1 hit
TIGRFAMsiTIGR00546 lnt, 1 hit
PROSITEiView protein in PROSITE
PS50263 CN_HYDROLASE, 1 hit

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, NZ_KK339370.1

Genome annotation databases

EnsemblBacteriaiCCP44824; CCP44824; Rv2051c
GeneIDi887402
KEGGimtu:Rv2051c
mtv:RVBD_2051c
PATRICifig|83332.111.peg.2287

Similar proteinsi

Entry informationi

Entry nameiPPMNT_MYCTU
AccessioniPrimary (citable) accession number: O53493
Secondary accession number(s): F2GDY6, I6Y888, L0TBC5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 11, 2015
Last sequence update: June 1, 1998
Last modified: March 28, 2018
This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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