UniProtKB - P24559 (PILT_PSEAE)
Protein
Type IV pilus retractation ATPase PilT
Gene
pilT
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Functioni
ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (PubMed:10377148, PubMed:15629932, PubMed:18174131). Acts as a molecular motor to provide the energy that is required for T4P retraction while antagonist PilB ATPase activity is required for T4P extension (PubMed:26809217). Promotes also PilU retractation activity through direct interaction (PubMed:31626631).5 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 82 | ATPCombined sources | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 133 – 138 | ATPCombined sources | 6 |
GO - Molecular functioni
- ATPase activity Source: PseudoCAP
- ATP binding Source: UniProtKB-KW
GO - Biological processi
- pilus retraction Source: PseudoCAP
- type IV pilus-dependent motility Source: PseudoCAP
Keywordsi
Biological process | Fimbrium biogenesis, Transport |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | PAER208964:G1FZ6-399-MONOMER |
Protein family/group databases
TCDBi | 3.A.15.2.1, the outer membrane protein secreting main terminal branch (mtb) family |
Names & Taxonomyi
Protein namesi | Recommended name: Type IV pilus retractation ATPase PilT1 Publication |
Gene namesi | Name:pilT Ordered Locus Names:PA0395 |
Organismi | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
Taxonomic identifieri | 208964 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › |
Proteomesi |
|
Organism-specific databases
PseudoCAPi | PA0395 |
Subcellular locationi
- Cytoplasm 1 Publication Note: Localizes to cell poles.1 Publication
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
- type IV pilus Source: PseudoCAP
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Mutants retain surface pili but have lost twitching motility (PubMed:15629932). In a mouse model of acute pneumonia, a decreased colonization of the liver is observed but not of the lung relative to the parental strain (PubMed:10377148).2 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 135 | G → S: Complete loss of ATPase activity and twitching activity. 1 Publication | 1 | |
Mutagenesisi | 136 | K → Q: Loss of motility. 1 Publication | 1 | |
Mutagenesisi | 163 | E → Q: About 50% loss of ATPase activity and twitching activity. 1 Publication | 1 | |
Mutagenesisi | 204 | E → Q: Complete loss of ATPase activity and twitching activity. 1 Publication | 1 | |
Mutagenesisi | 229 | H → A: About 80% loss of ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 288 | A → V: Loss of motility. 1 Publication | 1 | |
Mutagenesisi | 289 | I → A: Loss of motility. 1 Publication | 1 | |
Mutagenesisi | 292 | L → A: Loss of motility. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000207296 | 1 – 344 | Type IV pilus retractation ATPase PilTAdd BLAST | 344 |
Proteomic databases
PaxDbi | P24559 |
PRIDEi | P24559 |
Interactioni
Subunit structurei
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P24559 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P24559 |
Family & Domainsi
Domaini
The N-terminal region is responsible for proper localization to the piliated pole.1 Publication
Sequence similaritiesi
Belongs to the GSP E family.Curated
Phylogenomic databases
HOGENOMi | CLU_013446_4_0_6 |
InParanoidi | P24559 |
OMAi | ELDCSYG |
PhylomeDBi | P24559 |
Family and domain databases
CDDi | cd01131, PilT, 1 hit |
InterProi | View protein in InterPro IPR003593, AAA+_ATPase IPR027417, P-loop_NTPase IPR006321, PilT/PilU IPR001482, T2SS/T4SS |
Pfami | View protein in Pfam PF00437, T2SSE, 1 hit |
SMARTi | View protein in SMART SM00382, AAA, 1 hit |
SUPFAMi | SSF52540, SSF52540, 1 hit |
TIGRFAMsi | TIGR01420, pilT_fam, 1 hit |
PROSITEi | View protein in PROSITE PS00662, T2SP_E, 1 hit |
i Sequence
Sequence statusi: Complete.
P24559-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDITELLAFS AKQGASDLHL SAGLPPMIRV DGDVRRINLP PLEHKQVHAL
60 70 80 90 100
IYDIMNDKQR KDFEEFLETD FSFEVPGVAR FRVNAFNQNR GAGAVFRTIP
110 120 130 140 150
SKVLTMEELG MGEVFKRVSD VPRGLVLVTG PTGSGKSTTL AAMLDYLNNT
160 170 180 190 200
KYHHILTIED PIEFVHESKK CLVNQREVHR DTLGFSEALR SALREDPDII
210 220 230 240 250
LVGEMRDLET IRLALTAAET GHLVFGTLHT TSAAKTIDRV VDVFPAEEKA
260 270 280 290 300
MVRSMLSESL QSVISQTLIK KIGGGRVAAH EIMIGTPAIR NLIREDKVAQ
310 320 330 340
MYSAIQTGGS LGMQTLDMCL KGLVAKGLIS RENAREKAKI PENF
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M55524 Genomic DNA Translation: AAA25963.1 AE004091 Genomic DNA Translation: AAG03784.1 |
PIRi | JN0055 |
RefSeqi | NP_249086.1, NC_002516.2 WP_003084552.1, NZ_QZGE01000016.1 |
Genome annotation databases
EnsemblBacteriai | AAG03784; AAG03784; PA0395 |
GeneIDi | 878389 |
KEGGi | pae:PA0395 |
PATRICi | fig|208964.12.peg.416 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M55524 Genomic DNA Translation: AAA25963.1 AE004091 Genomic DNA Translation: AAG03784.1 |
PIRi | JN0055 |
RefSeqi | NP_249086.1, NC_002516.2 WP_003084552.1, NZ_QZGE01000016.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3JVU | X-ray | 3.10 | A/B/C | 1-344 | [»] | |
3JVV | X-ray | 2.60 | A/B/C | 1-344 | [»] | |
SMRi | P24559 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
TCDBi | 3.A.15.2.1, the outer membrane protein secreting main terminal branch (mtb) family |
Proteomic databases
PaxDbi | P24559 |
PRIDEi | P24559 |
Protocols and materials databases
DNASUi | 878389 |
Genome annotation databases
EnsemblBacteriai | AAG03784; AAG03784; PA0395 |
GeneIDi | 878389 |
KEGGi | pae:PA0395 |
PATRICi | fig|208964.12.peg.416 |
Organism-specific databases
PseudoCAPi | PA0395 |
Phylogenomic databases
HOGENOMi | CLU_013446_4_0_6 |
InParanoidi | P24559 |
OMAi | ELDCSYG |
PhylomeDBi | P24559 |
Enzyme and pathway databases
BioCyci | PAER208964:G1FZ6-399-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P24559 |
Family and domain databases
CDDi | cd01131, PilT, 1 hit |
InterProi | View protein in InterPro IPR003593, AAA+_ATPase IPR027417, P-loop_NTPase IPR006321, PilT/PilU IPR001482, T2SS/T4SS |
Pfami | View protein in Pfam PF00437, T2SSE, 1 hit |
SMARTi | View protein in SMART SM00382, AAA, 1 hit |
SUPFAMi | SSF52540, SSF52540, 1 hit |
TIGRFAMsi | TIGR01420, pilT_fam, 1 hit |
PROSITEi | View protein in PROSITE PS00662, T2SP_E, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PILT_PSEAE | |
Accessioni | P24559Primary (citable) accession number: P24559 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 1, 1992 |
Last sequence update: | March 1, 1992 | |
Last modified: | February 10, 2021 | |
This is version 126 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