PILT_PSEAE
ID PILT_PSEAE Reviewed; 344 AA.
AC P24559;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Type IV pilus retractation ATPase PilT {ECO:0000303|PubMed:15629932};
GN Name=pilT; OrderedLocusNames=PA0395;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1676385; DOI=10.1016/0378-1119(91)90221-v;
RA Whitchurch C.B., Hobbs M., Livingston S.P., Krishnapillai V., Mattick J.S.;
RT "Characterisation of a Pseudomonas aeruginosa twitching motility gene and
RT evidence for a specialised protein export system widespread in
RT eubacteria.";
RL Gene 101:33-44(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAK;
RX PubMed=10377148; DOI=10.1128/iai.67.7.3625-3630.1999;
RA Comolli J.C., Hauser A.R., Waite L., Whitchurch C.B., Mattick J.S.,
RA Engel J.N.;
RT "Pseudomonas aeruginosa gene products PilT and PilU are required for
RT cytotoxicity in vitro and virulence in a mouse model of acute pneumonia.";
RL Infect. Immun. 67:3625-3630(1999).
RN [4]
RP FUNCTION, MUTAGENESIS OF LYS-136; ALA-288; ILE-289 AND LEU-292, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=PAK;
RX PubMed=15629932; DOI=10.1128/jb.187.2.611-618.2005;
RA Aukema K.G., Kron E.M., Herdendorf T.J., Forest K.T.;
RT "Functional dissection of a conserved motif within the pilus retraction
RT protein PilT.";
RL J. Bacteriol. 187:611-618(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15659660; DOI=10.1128/jb.187.3.829-839.2005;
RA Chiang P., Habash M., Burrows L.L.;
RT "Disparate subcellular localization patterns of Pseudomonas aeruginosa Type
RT IV pilus ATPases involved in twitching motility.";
RL J. Bacteriol. 187:829-839(2005).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-135; GLU-163; GLU-204 AND HIS-229.
RX PubMed=18174131; DOI=10.1099/mic.0.2007/011320-0;
RA Chiang P., Sampaleanu L.M., Ayers M., Pahuta M., Howell P.L., Burrows L.L.;
RT "Functional role of conserved residues in the characteristic secretion
RT NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins
RT PilB, PilT and PilU.";
RL Microbiology 154:114-126(2008).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=31626631; DOI=10.1371/journal.pgen.1008448;
RA Chlebek J.L., Hughes H.Q., Ratkiewicz A.S., Rayyan R., Wang J.C.,
RA Herrin B.E., Dalia T.N., Biais N., Dalia A.B.;
RT "PilT and PilU are homohexameric ATPases that coordinate to retract type
RT IVa pili.";
RL PLoS Genet. 15:e1008448-e1008448(2019).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=26809217; DOI=10.1016/j.jiac.2015.12.012;
RA Shikata M., Hayashi N., Fujimoto A., Nakamura T., Matsui N., Ishiyama A.,
RA Maekawa Y., Gotoh N.;
RT "The pilT gene contributes to type III ExoS effector injection into
RT epithelial cells in Pseudomonas aeruginosa.";
RL J. Infect. Chemother. 22:216-220(2016).
RN [9] {ECO:0007744|PDB:3JVU, ECO:0007744|PDB:3JVV}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, AND
RP SUBUNIT.
RX PubMed=20595000; DOI=10.1016/j.jmb.2010.05.066;
RA Misic A.M., Satyshur K.A., Forest K.T.;
RT "P. aeruginosa PilT structures with and without nucleotide reveal a dynamic
RT type IV pilus retraction motor.";
RL J. Mol. Biol. 400:1011-1021(2010).
CC -!- FUNCTION: ATPase component of the type IV pilus (T4P) that plays a role
CC in surface and host cell adhesion, colonization, biofilm maturation,
CC virulence, and twitching, a form of surface-associated motility
CC facilitated by cycles of extension, adhesion, and retraction of T4P
CC fibers (PubMed:10377148, PubMed:15629932, PubMed:18174131). Acts as a
CC molecular motor to provide the energy that is required for T4P
CC retraction while antagonist PilB ATPase activity is required for T4P
CC extension (PubMed:26809217). Promotes also PilU retractation activity
CC through direct interaction (PubMed:31626631).
CC {ECO:0000269|PubMed:10377148, ECO:0000269|PubMed:15629932,
CC ECO:0000269|PubMed:18174131, ECO:0000269|PubMed:26809217,
CC ECO:0000269|PubMed:31626631}.
CC -!- SUBUNIT: Homohexamer (PubMed:31626631). Interacts with PilU (Probable).
CC {ECO:0000269|PubMed:31626631, ECO:0000305|PubMed:31626631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15659660}.
CC Note=Localizes to cell poles. {ECO:0000269|PubMed:15659660}.
CC -!- DOMAIN: The N-terminal region is responsible for proper localization to
CC the piliated pole. {ECO:0000269|PubMed:15659660}.
CC -!- DISRUPTION PHENOTYPE: Mutants retain surface pili but have lost
CC twitching motility (PubMed:15629932). In a mouse model of acute
CC pneumonia, a decreased colonization of the liver is observed but not of
CC the lung relative to the parental strain (PubMed:10377148).
CC {ECO:0000269|PubMed:10377148, ECO:0000269|PubMed:15629932}.
CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR EMBL; M55524; AAA25963.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03784.1; -; Genomic_DNA.
DR PIR; JN0055; JN0055.
DR RefSeq; NP_249086.1; NC_002516.2.
DR RefSeq; WP_003084552.1; NZ_QZGE01000016.1.
DR PDB; 3JVU; X-ray; 3.10 A; A/B/C=1-344.
DR PDB; 3JVV; X-ray; 2.60 A; A/B/C=1-344.
DR PDBsum; 3JVU; -.
DR PDBsum; 3JVV; -.
DR AlphaFoldDB; P24559; -.
DR SMR; P24559; -.
DR STRING; 287.DR97_3363; -.
DR TCDB; 3.A.15.2.1; the outer membrane protein secreting main terminal branch (mtb) family.
DR PaxDb; P24559; -.
DR PRIDE; P24559; -.
DR DNASU; 878389; -.
DR EnsemblBacteria; AAG03784; AAG03784; PA0395.
DR GeneID; 878389; -.
DR KEGG; pae:PA0395; -.
DR PATRIC; fig|208964.12.peg.416; -.
DR PseudoCAP; PA0395; -.
DR HOGENOM; CLU_013446_4_0_6; -.
DR InParanoid; P24559; -.
DR OMA; WELDCSY; -.
DR PhylomeDB; P24559; -.
DR BioCyc; PAER208964:G1FZ6-399-MON; -.
DR EvolutionaryTrace; P24559; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044096; C:type IV pilus; TAS:PseudoCAP.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:PseudoCAP.
DR GO; GO:0043108; P:pilus retraction; TAS:PseudoCAP.
DR GO; GO:0043107; P:type IV pilus-dependent motility; TAS:PseudoCAP.
DR CDD; cd01131; PilT; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006321; PilT/PilU.
DR InterPro; IPR001482; T2SS/T4SS.
DR Pfam; PF00437; T2SSE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01420; pilT_fam; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Fimbrium biogenesis;
KW Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1..344
FT /note="Type IV pilus retractation ATPase PilT"
FT /id="PRO_0000207296"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:3JVV"
FT BINDING 133..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:3JVV"
FT MUTAGEN 135
FT /note="G->S: Complete loss of ATPase activity and twitching
FT activity."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 136
FT /note="K->Q: Loss of motility."
FT /evidence="ECO:0000269|PubMed:15629932"
FT MUTAGEN 163
FT /note="E->Q: About 50% loss of ATPase activity and
FT twitching activity."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 204
FT /note="E->Q: Complete loss of ATPase activity and twitching
FT activity."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 229
FT /note="H->A: About 80% loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 288
FT /note="A->V: Loss of motility."
FT /evidence="ECO:0000269|PubMed:15629932"
FT MUTAGEN 289
FT /note="I->A: Loss of motility."
FT /evidence="ECO:0000269|PubMed:15629932"
FT MUTAGEN 292
FT /note="L->A: Loss of motility."
FT /evidence="ECO:0000269|PubMed:15629932"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:3JVV"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:3JVV"
FT TURN 106..110
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:3JVV"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:3JVV"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:3JVV"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:3JVV"
SQ SEQUENCE 344 AA; 38021 MW; C35F89F28AD0BE01 CRC64;
MDITELLAFS AKQGASDLHL SAGLPPMIRV DGDVRRINLP PLEHKQVHAL IYDIMNDKQR
KDFEEFLETD FSFEVPGVAR FRVNAFNQNR GAGAVFRTIP SKVLTMEELG MGEVFKRVSD
VPRGLVLVTG PTGSGKSTTL AAMLDYLNNT KYHHILTIED PIEFVHESKK CLVNQREVHR
DTLGFSEALR SALREDPDII LVGEMRDLET IRLALTAAET GHLVFGTLHT TSAAKTIDRV
VDVFPAEEKA MVRSMLSESL QSVISQTLIK KIGGGRVAAH EIMIGTPAIR NLIREDKVAQ
MYSAIQTGGS LGMQTLDMCL KGLVAKGLIS RENAREKAKI PENF
