PILU_PSEAE
ID PILU_PSEAE Reviewed; 382 AA.
AC G3XCX3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Type IV pilus ATPase PilU;
GN Name=pilU; OrderedLocusNames=PA0396;
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 [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 [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7854122; DOI=10.1111/j.1365-2958.1994.tb00499.x;
RA Whitchurch C.B., Mattick J.S.;
RT "Characterization of a gene, pilU, required for twitching motility but not
RT phage sensitivity in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 13:1079-1091(1994).
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 SUBCELLULAR LOCATION, AND DOMAIN.
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 [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-135; GLU-159; ASP-160; GLU-163; GLU-204
RP 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 [6]
RP FUNCTION.
RX PubMed=31525185; DOI=10.1371/journal.pgen.1008393;
RA Adams D.W., Pereira J.M., Stoudmann C., Stutzmann S., Blokesch M.;
RT "The type IV pilus protein PilU functions as a PilT-dependent retraction
RT ATPase.";
RL PLoS Genet. 15:e1008393-e1008393(2019).
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).
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:7854122, PubMed:10377148, PubMed:15659660,
CC PubMed:18174131). Functions as a PilT-dependent retraction ATPase,
CC providing a functional coupling between PilT and PilU and an optimal
CC mechanism for pilus retraction (PubMed:31525185, PubMed:31626631).
CC {ECO:0000269|PubMed:10377148, ECO:0000269|PubMed:15659660,
CC ECO:0000269|PubMed:18174131, ECO:0000269|PubMed:31525185,
CC ECO:0000269|PubMed:31626631, ECO:0000269|PubMed:7854122}.
CC -!- SUBUNIT: Homohexamer (PubMed:31626631). Interacts with PilT (Probable).
CC {ECO:0000269|PubMed:31626631, ECO:0000305|PubMed:31525185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15659660}.
CC Note=Localizes only to the piliated pole.
CC {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 are hyperfimbriate, retain surface pili
CC but have lost twitching motility (PubMed:7854122). In a mouse model of
CC acute pneumonia, a decreased colonization of the liver is observed but
CC not of the lung relative to the parental strain (PubMed:10377148).
CC {ECO:0000269|PubMed:10377148, ECO:0000269|PubMed:7854122}.
CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR EMBL; AE004091; AAG03785.1; -; Genomic_DNA.
DR PIR; S54702; S54702.
DR RefSeq; NP_249087.1; NC_002516.2.
DR RefSeq; WP_003100959.1; NZ_QZGE01000016.1.
DR AlphaFoldDB; G3XCX3; -.
DR SMR; G3XCX3; -.
DR STRING; 287.DR97_3364; -.
DR PaxDb; G3XCX3; -.
DR PRIDE; G3XCX3; -.
DR EnsemblBacteria; AAG03785; AAG03785; PA0396.
DR GeneID; 878362; -.
DR KEGG; pae:PA0396; -.
DR PATRIC; fig|208964.12.peg.417; -.
DR PseudoCAP; PA0396; -.
DR HOGENOM; CLU_013446_4_0_6; -.
DR InParanoid; G3XCX3; -.
DR OMA; QGLCRTT; -.
DR PhylomeDB; G3XCX3; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IDA:PseudoCAP.
DR GO; GO:0043107; P:type IV pilus-dependent motility; IMP:PseudoCAP.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006321; PilT/PilU.
DR InterPro; IPR001482; T2SS/T4SS.
DR Pfam; PF00437; T2SSE; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01420; pilT_fam; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..382
FT /note="Type IV pilus ATPase PilU"
FT /id="PRO_0000450555"
FT BINDING 133..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24559"
FT MUTAGEN 135
FT /note="G->S: Loss of twitching motility but no change in
FT unipolar localization."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 159
FT /note="E->Q: Loss of twitching motility but no change in
FT unipolar localization."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 160
FT /note="D->N: Loss of twitching motility but no change in
FT unipolar localization."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 163
FT /note="E->Q: Loss of twitching motility but no change in
FT unipolar localization."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 204
FT /note="E->Q: Loss of twitching motility but no change in
FT unipolar localization."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 229
FT /note="H->A: Loss of twitching motility but no change in
FT unipolar localization."
FT /evidence="ECO:0000269|PubMed:18174131"
SQ SEQUENCE 382 AA; 42533 MW; 0266E5D0FED35E17 CRC64;
MEFEKLLRLM VEKGGSDLFI TAGVPPSMKV NGRVMPVTKT PLSPEQTRET VLGVMNEQQR
RDFAENHECN FAISARGIGR FRVSAFYQRN LVGMVLRRIE TNIPTLEELK LPEILKKLAL
TKRGLVIFVG ATGTGKSTSL AAMIGYRNKN STGHIISIED PIEYIHQHQG CIVTQREVGL
DTDSFEVALK NTLRQAPDVI MIGEVRSRET MDHAVAFAET GHLCLATLHA NNANQALERI
IHFFPADRHG QVWMDLSLNL KAIVAQQLVP TPDGKGRRAV IEVLLNTPLA ADLIRKGEVH
ELKPLMKRST EQGMQTFDQA LYQLYTQGEI TYEDALAHAD SANDLRLMIK LGSESDADHL
SSLTQGLSLE ITDDDPAGRR FR
