UniProtKB - P9WIK5 (PAPA3_MYCTU)
Protein
Acyltransferase PapA3
Gene
papA3
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Involved in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid that could have a role in anchoring the bacterial capsule. Catalyzes the sequential transfer of two palmitoyl groups onto a single glucose residue of trehalose generating the diacylated product 2,3-diacyltrehalose (trehalose dipalmitate). Although palmitoyl-CoA (PCoA) seems to be the physiological acyl donor, PapA3 can also use docosanoyl (22-carbon saturated fatty acid) coenzyme A as acyl donor.1 Publication
Catalytic activityi
- a long-chain fatty acyl-CoA + α,α-trehalose = 2-O-(long-chain fatty acyl)-α,α-trehalose + CoA1 PublicationEC:2.3.1.2791 PublicationThis reaction proceeds in the forward1 Publication direction.
- 2-O-(long-chain fatty acyl)-α,α-trehalose + a mycolipenoyl-CoA = 2-O-(long-chain fatty acyl)-3-O-mycolipenoyl-trehalose + CoA1 PublicationEC:2.3.1.2781 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- 2-O-hexadecanoyl-α,α-trehalose + hexadecanoyl-CoA = 2-O,3-O-dihexadecanoyl-α,α-trehalose + CoA1 PublicationThis reaction proceeds in the forward1 Publication direction.
GO - Molecular functioni
- palmitoyltransferase activity Source: MTBBASE
GO - Biological processi
- glycolipid biosynthetic process Source: MTBBASE
- trehalose metabolic process Source: MTBBASE
Keywordsi
Molecular function | Acyltransferase, Transferase |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-5351-MONOMER |
Chemistry databases
SwissLipidsi | SLP:000001028 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:papA3 Ordered Locus Names:Rv1182 |
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 | Rv1182 |
Pathology & Biotechi
Disruption phenotypei
Deletion of the gene prevents PAT synthesis.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000420764 | 1 – 472 | Acyltransferase PapA3Add BLAST | 472 |
Proteomic databases
PaxDbi | P9WIK5 |
PRIDEi | P9WIK5 |
Family & Domainsi
Sequence similaritiesi
Belongs to the PapA acyltransferase family.Curated
Phylogenomic databases
eggNOGi | COG1020, Bacteria |
OMAi | ANNIGIY |
PhylomeDBi | P9WIK5 |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit |
InterProi | View protein in InterPro IPR023213, CAT-like_dom_sf IPR001242, Condensatn |
Pfami | View protein in Pfam PF00668, Condensation, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WIK5-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLRVGPLTIG TLDDWAPSTG STVSWRPSAV AHTKASQAPI SDVPVSYMQA
60 70 80 90 100
QHIRGYCEQK AKGLDYSRLM VVSCQQPGQC DIRAANYVIN AHLRRHDTYR
110 120 130 140 150
SWFQYNGNGQ IIRRTIQDPA DIEFVPVHHG ELTLPQIREI VQNTPDPLQW
160 170 180 190 200
GCFRFGIVQG CDHFTFFASV DHVHVDAMIV GVTLMEFHLM YAALVGGHAP
210 220 230 240 250
LELPPAGSYD DFCRRQHTFS STLTVESPQV RAWTKFAEGT NGSFPDFPLP
260 270 280 290 300
LGDPSKPSDA DIVTVMMLDE EQTAQFESVC TAAGARFIGG VLACCGLAEH
310 320 330 340 350
ELTGTTTYYG LTPRDTRRTP ADAMTQGWFT GLIPITVPIA GSAFGDAARA
360 370 380 390 400
AQTSFDSGVK LAEVPYDRVV ELSSTLTMPR PNFPVVNFLD AGAAPLSVLL
410 420 430 440 450
TAELTGTNIG VYSDGRYSYQ LSIYVIRVEQ GTAVAVMFPD NPIARESVAR
460 470
YLATLKSVFQ RVAESGQQQN VA
Mass spectrometryi
Molecular mass is 51809 Da. Determined by ESI. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43938.1 |
PIRi | F70876 |
RefSeqi | NP_215698.1, NC_000962.3 WP_003898759.1, NZ_NVQJ01000025.1 |
Genome annotation databases
EnsemblBacteriai | CCP43938; CCP43938; Rv1182 |
GeneIDi | 45425153 886072 |
KEGGi | mtu:Rv1182 |
PATRICi | fig|83332.111.peg.1322 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43938.1 |
PIRi | F70876 |
RefSeqi | NP_215698.1, NC_000962.3 WP_003898759.1, NZ_NVQJ01000025.1 |
3D structure databases
SMRi | P9WIK5 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv1182 |
Chemistry databases
SwissLipidsi | SLP:000001028 |
Proteomic databases
PaxDbi | P9WIK5 |
PRIDEi | P9WIK5 |
Genome annotation databases
EnsemblBacteriai | CCP43938; CCP43938; Rv1182 |
GeneIDi | 45425153 886072 |
KEGGi | mtu:Rv1182 |
PATRICi | fig|83332.111.peg.1322 |
Organism-specific databases
TubercuListi | Rv1182 |
Phylogenomic databases
eggNOGi | COG1020, Bacteria |
OMAi | ANNIGIY |
PhylomeDBi | P9WIK5 |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-5351-MONOMER |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit |
InterProi | View protein in InterPro IPR023213, CAT-like_dom_sf IPR001242, Condensatn |
Pfami | View protein in Pfam PF00668, Condensation, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PAPA3_MYCTU | |
Accessioni | P9WIK5Primary (citable) accession number: P9WIK5 Secondary accession number(s): F2GG06 Q7D8P1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | February 10, 2021 | |
This is version 36 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
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families