PILF_PSEAE
ID PILF_PSEAE Reviewed; 252 AA.
AC Q9HXJ2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Type IV pilus assembly protein PilF;
DE Flags: Precursor;
GN Name=pilF; OrderedLocusNames=PA3805;
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=8973346; DOI=10.1016/s0378-1119(96)00403-9;
RA Watson A.A., Alm R.A., Mattick J.S.;
RT "Identification of a gene, pilF, required for type 4 fimbrial biogenesis
RT and twitching motility in Pseudomonas aeruginosa.";
RL Gene 180:49-56(1996).
RN [3]
RP FUNCTION, DOMAIN, AND INTERACTION WITH PILQ.
RX PubMed=23547883; DOI=10.1021/bi3015345;
RA Koo J., Tang T., Harvey H., Tammam S., Sampaleanu L., Burrows L.L.,
RA Howell P.L.;
RT "Functional mapping of PilF and PilQ in the Pseudomonas aeruginosa type IV
RT pilus system.";
RL Biochemistry 52:2914-2923(2013).
RN [4] {ECO:0007744|PDB:2FI7}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-252, AND DOMAIN.
RX PubMed=16403447; DOI=10.1016/j.bbrc.2005.12.108;
RA Kim K., Oh J., Han D., Kim E.E., Lee B., Kim Y.;
RT "Crystal structure of PilF: functional implication in the type 4 pilus
RT biogenesis in Pseudomonas aeruginosa.";
RL Biochem. Biophys. Res. Commun. 340:1028-1038(2006).
RN [5] {ECO:0007744|PDB:2HO1}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 22-252, FUNCTION, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, DOMAIN, AND MUTAGENESIS OF CYS-18.
RX PubMed=18776008; DOI=10.1128/jb.00996-08;
RA Koo J., Tammam S., Ku S.Y., Sampaleanu L.M., Burrows L.L., Howell P.L.;
RT "PilF is an outer membrane lipoprotein required for multimerization and
RT localization of the Pseudomonas aeruginosa Type IV pilus secretin.";
RL J. Bacteriol. 190:6961-6969(2008).
CC -!- FUNCTION: Essential component of the type IV pilus (T4P) that plays a
CC role in surface and host cell adhesion, colonization, biofilm
CC maturation, virulence, and twitching, a form of surface-associated
CC motility facilitated by cycles of extension, adhesion, and retraction
CC of T4P fibers (PubMed:8973346). Plays an essential role in the outer
CC membrane localization and assembly of PilQ into secretins which are
CC dodecamers of PilQ (PubMed:23547883, PubMed:18776008).
CC {ECO:0000269|PubMed:18776008, ECO:0000269|PubMed:23547883,
CC ECO:0000269|PubMed:8973346}.
CC -!- SUBUNIT: Interacts with PilQ; this interaction is essential for assemby
CC of PilQ into secretins. {ECO:0000269|PubMed:23547883}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:18776008}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}.
CC -!- DOMAIN: Contains six tetratricopeptide (TPR) protein-protein
CC interaction motifs (PubMed:23547883, PubMed:16403447, PubMed:18776008).
CC TPR1-TPR4 form the minimal region required for secretin assembly and
CC function (PubMed:23547883). {ECO:0000269|PubMed:16403447,
CC ECO:0000269|PubMed:18776008, ECO:0000269|PubMed:23547883}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows an impaired export/assembly of the
CC fimbrial subunit PilA, and accumulates this protein in the membrane
CC fraction (PubMed:8973346). In addition, loss of PilF expression
CC abolishes multimerization of PilQ (PubMed:18776008).
CC {ECO:0000269|PubMed:18776008, ECO:0000269|PubMed:8973346}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG07192.1; -; Genomic_DNA.
DR PIR; H83171; H83171.
DR RefSeq; NP_252494.1; NC_002516.2.
DR RefSeq; WP_003113801.1; NZ_QZGE01000001.1.
DR PDB; 2FI7; X-ray; 2.20 A; A/B=20-252.
DR PDB; 2HO1; X-ray; 2.00 A; A/B=11-252.
DR PDBsum; 2FI7; -.
DR PDBsum; 2HO1; -.
DR AlphaFoldDB; Q9HXJ2; -.
DR SMR; Q9HXJ2; -.
DR STRING; 287.DR97_4064; -.
DR PaxDb; Q9HXJ2; -.
DR PRIDE; Q9HXJ2; -.
DR DNASU; 879170; -.
DR EnsemblBacteria; AAG07192; AAG07192; PA3805.
DR GeneID; 879170; -.
DR KEGG; pae:PA3805; -.
DR PATRIC; fig|208964.12.peg.3984; -.
DR PseudoCAP; PA3805; -.
DR HOGENOM; CLU_003728_7_1_6; -.
DR InParanoid; Q9HXJ2; -.
DR OMA; YPGTPEY; -.
DR PhylomeDB; Q9HXJ2; -.
DR BioCyc; PAER208964:G1FZ6-3876-MON; -.
DR EvolutionaryTrace; Q9HXJ2; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030911; F:TPR domain binding; IDA:PseudoCAP.
DR GO; GO:0009297; P:pilus assembly; IDA:PseudoCAP.
DR GO; GO:0046903; P:secretion; IDA:PseudoCAP.
DR GO; GO:0043683; P:type IV pilus assembly; IDA:PseudoCAP.
DR GO; GO:0043107; P:type IV pilus-dependent motility; IDA:PseudoCAP.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013360; Pilus_4_PilW.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR02521; type_IV_pilW; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Repeat; Signal; TPR repeat.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..252
FT /note="Type IV pilus assembly protein PilF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5004326874"
FT REPEAT 32..67
FT /note="TPR 1"
FT /evidence="ECO:0000305|PubMed:16403447,
FT ECO:0000305|PubMed:18776008"
FT REPEAT 84..101
FT /note="TPR 2"
FT /evidence="ECO:0000305|PubMed:16403447,
FT ECO:0000305|PubMed:18776008"
FT REPEAT 104..133
FT /note="TPR 3"
FT /evidence="ECO:0000305|PubMed:16403447,
FT ECO:0000305|PubMed:18776008"
FT REPEAT 139..171
FT /note="TPR 4"
FT /evidence="ECO:0000305|PubMed:16403447,
FT ECO:0000305|PubMed:18776008"
FT REPEAT 174..203
FT /note="TPR 5"
FT /evidence="ECO:0000305|PubMed:16403447,
FT ECO:0000305|PubMed:18776008"
FT REPEAT 208..235
FT /note="TPR 6"
FT /evidence="ECO:0000305|PubMed:16403447,
FT ECO:0000305|PubMed:18776008"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 18
FT /note="C->G: Loss of association with the outer membrane.
FT PilQ multimers were detected not only in the outer membrane
FT but also in the inner membrane and the soluble lysate."
FT /evidence="ECO:0000269|PubMed:18776008"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:2HO1"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:2HO1"
SQ SEQUENCE 252 AA; 28537 MW; F7480FA80636CEC9 CRC64;
MTVRAALVFL LAVGLTGCVT SGDQNPLKTD KGRDEARDAY IQLGLGYLQR GNTEQAKVPL
RKALEIDPSS ADAHAALAVV FQTEMEPKLA DEEYRKALAS DSRNARVLNN YGGFLYEQKR
YEEAYQRLLE ASQDTLYPER SRVFENLGLV SLQMKKPAQA KEYFEKSLRL NRNQPSVALE
MADLLYKERE YVPARQYYDL FAQGGGQNAR SLLLGIRLAK VFEDRDTAAS YGLQLKRLYP
GSLEYQEFQA EK
