UniProtKB - O33336 (PPTT_MYCTU)
Protein
4'-phosphopantetheinyl transferase PptT
Gene
pptT
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein (PubMed:9831524, PubMed:16709676, PubMed:25785780, PubMed:28203522). Involved in post-translational modification of various type-I polyketide synthases required for the formation of both mycolic acids and lipid virulence factors (PubMed:16709676). Acts on Pks13, Mas, PpsA, PpsB, PpsC and PpsD (PubMed:16709676, PubMed:28203522). Also acts on AcpM, the meromycolate extension acyl carrier protein (PubMed:25785780). In addition, is involved in the activation of the acyl carrier protein MbtL and the nonribosomal peptides synthases MbtB and MbtE, which are involved in the biosynthesis of the siderophore mycobactin (PubMed:9831524, PubMed:28203522).4 Publications
Required for the replication and survival of Mycobacterium during the acute and chronic phases of infection in mice.1 Publication
Miscellaneous
Identified as a drug target.1 Publication
Catalytic activityi
- EC:2.7.8.74 Publications
Cofactori
Mg2+1 Publication
Activity regulationi
Inhibited by the amidino-urea compound 1-[(2,6-diethylphenyl)-3-N-ethylcarbamimodoyl]urea (compound 8918). It acts by binding to the phosphopantetheine pocket in the active site. Inhibition by compound 8918 kills M.tuberculosis.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 48 | Coenzyme A3 Publications | 1 | |
Binding sitei | 56 | Coenzyme A3 Publications | 1 | |
Metal bindingi | 114 | MagnesiumCombined sources1 Publication | 1 | |
Binding sitei | 114 | Coenzyme A2 Publications | 1 | |
Metal bindingi | 115 | Magnesium; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 116 | MagnesiumCombined sources1 Publication | 1 | |
Binding sitei | 157 | Coenzyme A2 Publications | 1 | |
Binding sitei | 161 | Coenzyme A3 Publications | 1 | |
Binding sitei | 171 | Coenzyme A; via carbonyl oxygen3 Publications | 1 |
GO - Molecular functioni
- holo-[acyl-carrier-protein] synthase activity Source: MTBBASE
- magnesium ion binding Source: InterPro
GO - Biological processi
- enterobactin biosynthetic process Source: InterPro
- siderophore biosynthetic process Source: UniProtKB
- siderophore metabolic process Source: GO_Central
Keywordsi
Molecular function | Transferase |
Ligand | Magnesium, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: 4'-phosphopantetheinyl transferase PptTCurated (EC:2.7.8.74 Publications)Short name: PPTase1 Publication |
Gene namesi | Name:pptT1 Publication Ordered Locus Names:Rv2794cImported |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv2794c |
Subcellular locationi
GO - Cellular componenti
- enterobactin synthetase complex Source: InterPro
- intrinsic component of plasma membrane Source: GO_Central
- plasma membrane Source: MTBBASE
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 48 | R → A: 20-fold decrease in phosphopantetheinylation activity. 1 Publication | 1 | |
Mutagenesisi | 56 | R → A: 100-fold decrease in phosphopantetheinylation activity. 1 Publication | 1 | |
Mutagenesisi | 114 | D → N: Abolishes phosphopantetheinylation activity. 1 Publication | 1 | |
Mutagenesisi | 116 | E → Q: 500-fold decrease in phosphopantetheinylation activity. 1 Publication | 1 | |
Mutagenesisi | 157 | E → Q: Abolishes phosphopantetheinylation activity. 1 Publication | 1 | |
Mutagenesisi | 170 | W → L or S: Confers high-level resistance to compound 8918. 1 Publication | 1 |
Miscellaneous databases
PHI-basei | PHI:2629 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000451441 | 1 – 227 | 4'-phosphopantetheinyl transferase PptTAdd BLAST | 227 |
Proteomic databases
PaxDbi | O33336 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 75 – 78 | Coenzyme A binding3 Publications | 4 | |
Regioni | 92 – 93 | Coenzyme A binding3 Publications | 2 |
Sequence similaritiesi
Belongs to the P-Pant transferase superfamily.Curated
Phylogenomic databases
eggNOGi | COG2977, Bacteria |
OMAi | GSLTHCD |
Family and domain databases
InterProi | View protein in InterPro IPR008278, 4-PPantetheinyl_Trfase_dom IPR037143, 4-PPantetheinyl_Trfase_dom_sf IPR041354, 4PPT_N IPR003542, Enbac_synth_compD-like |
PANTHERi | PTHR38096, PTHR38096, 1 hit |
Pfami | View protein in Pfam PF17837, 4PPT_N, 1 hit PF01648, ACPS, 1 hit |
PRINTSi | PR01399, ENTSNTHTASED |
SUPFAMi | SSF56214, SSF56214, 1 hit |
i Sequence
Sequence statusi: Complete.
O33336-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTVGTLVASV LPATVFEDLA YAELYSDPPG LTPLPEEAPL IARSVAKRRN
60 70 80 90 100
EFITVRHCAR IALDQLGVPP APILKGDKGE PCWPDGMVGS LTHCAGYRGA
110 120 130 140 150
VVGRRDAVRS VGIDAEPHDV LPNGVLDAIS LPAERADMPR TMPAALHWDR
160 170 180 190 200
ILFCAKEATY KAWFPLTKRW LGFEDAHITF ETDSTGWTGR FVSRILIDGS
210 220
TLSGPPLTTL RGRWSVERGL VLTAIVL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45593.1 |
RefSeqi | NP_217310.1, NC_000962.3 WP_003917055.1, NZ_NVQJ01000020.1 |
Genome annotation databases
EnsemblBacteriai | AIR15566; AIR15566; LH57_15260 CCP45593; CCP45593; Rv2794c |
GeneIDi | 23490971 888226 |
KEGGi | mtu:Rv2794c mtv:RVBD_2794c |
PATRICi | fig|83332.111.peg.3107 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45593.1 |
RefSeqi | NP_217310.1, NC_000962.3 WP_003917055.1, NZ_NVQJ01000020.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4QJK | X-ray | 1.59 | A | 1-227 | [»] | |
4QVH | X-ray | 1.75 | A/B | 1-227 | [»] | |
4U89 | X-ray | 1.40 | A | 1-227 | [»] | |
6CT5 | X-ray | 1.76 | A/B | 1-227 | [»] | |
SMRi | O33336 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv2794c |
Proteomic databases
PaxDbi | O33336 |
Genome annotation databases
EnsemblBacteriai | AIR15566; AIR15566; LH57_15260 CCP45593; CCP45593; Rv2794c |
GeneIDi | 23490971 888226 |
KEGGi | mtu:Rv2794c mtv:RVBD_2794c |
PATRICi | fig|83332.111.peg.3107 |
Organism-specific databases
TubercuListi | Rv2794c |
Phylogenomic databases
eggNOGi | COG2977, Bacteria |
OMAi | GSLTHCD |
Miscellaneous databases
PHI-basei | PHI:2629 |
Family and domain databases
InterProi | View protein in InterPro IPR008278, 4-PPantetheinyl_Trfase_dom IPR037143, 4-PPantetheinyl_Trfase_dom_sf IPR041354, 4PPT_N IPR003542, Enbac_synth_compD-like |
PANTHERi | PTHR38096, PTHR38096, 1 hit |
Pfami | View protein in Pfam PF17837, 4PPT_N, 1 hit PF01648, ACPS, 1 hit |
PRINTSi | PR01399, ENTSNTHTASED |
SUPFAMi | SSF56214, SSF56214, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PPTT_MYCTU | |
Accessioni | O33336Primary (citable) accession number: O33336 Secondary accession number(s): I6XFB3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 2, 2020 |
Last sequence update: | January 1, 1998 | |
Last modified: | December 2, 2020 | |
This is version 129 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families