PILA_PSEAE
ID PILA_PSEAE Reviewed; 149 AA.
AC P04739;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Type IV major pilin protein PilA;
DE AltName: Full=Pilin;
DE Flags: Precursor;
GN Name=pilA; Synonyms=fimA; OrderedLocusNames=PA4525;
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=PAO;
RX PubMed=2997119; DOI=10.1128/jb.164.2.571-577.1985;
RA Sastry P.A., Finlay B.B., Pasloske B.L., Paranchych W., Pearlstone J.R.,
RA Smillie L.B.;
RT "Comparative studies of the amino acid and nucleotide sequences of pilin
RT derived from Pseudomonas aeruginosa PAK and PAO.";
RL J. Bacteriol. 164:571-577(1985).
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 METHYLATION AT PHE-7, AND MUTAGENESIS OF GLU-11.
RX PubMed=8330261; DOI=10.1139/m93-071;
RA Macdonald D.L., Pasloske B.L., Paranchych W.;
RT "Mutations in the fifth-position glutamate in Pseudomonas aeruginosa pilin
RT affect the transmethylation of the N-terminal phenylalanine.";
RL Can. J. Microbiol. 39:500-505(1993).
RN [4]
RP STRUCTURE BY NMR OF 132-149.
RX PubMed=8845350; DOI=10.1021/bi00050a005;
RA Campbell A.P., McInnes C., Hodges R.S., Sykes B.D.;
RT "Comparison of NMR solution structures of the receptor binding domains of
RT Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for
RT receptor binding and synthetic vaccine design.";
RL Biochemistry 34:16255-16268(1995).
RN [5]
RP CLEAVAGE BY PILD, AND MUTAGENESIS OF PHE-7.
RX PubMed=1429457; DOI=10.1128/jb.174.22.7345-7351.1992;
RA Strom M.S., Lory S.;
RT "Kinetics and sequence specificity of processing of prepilin by PilD, the
RT type IV leader peptidase of Pseudomonas aeruginosa.";
RL J. Bacteriol. 174:7345-7351(1992).
RN [6]
RP INTERACTION WITH XCPT; XCPU AND XCPW, DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=PAK;
RX PubMed=9282737; DOI=10.1046/j.1365-2958.1997.4561818.x;
RA Lu H.M., Motley S.T., Lory S.;
RT "Interactions of the components of the general secretion pathway: role of
RT Pseudomonas aeruginosa type IV pilin subunits in complex formation and
RT extracellular protein secretion.";
RL Mol. Microbiol. 25:247-259(1997).
RN [7]
RP FUNCTION, INTERACTION WITH HOST CAMLG, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=23266901; DOI=10.1007/s10156-012-0536-y;
RA Okuda J., Hayashi N., Arakawa M., Minagawa S., Gotoh N.;
RT "Type IV pilus protein PilA of Pseudomonas aeruginosa modulates calcium
RT signaling through binding the calcium-modulating cyclophilin ligand.";
RL J. Infect. Chemother. 19:653-664(2013).
RN [8]
RP FUNCTION, AND INTERACTION WITH PILJ.
RX PubMed=26041805; DOI=10.1073/pnas.1502025112;
RA Persat A., Inclan Y.F., Engel J.N., Stone H.A., Gitai Z.;
RT "Type IV pili mechanochemically regulate virulence factors in Pseudomonas
RT aeruginosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:7563-7568(2015).
RN [9]
RP INTERACTION WITH PILS, AND SUBCELLULAR LOCATION.
RX PubMed=27162347; DOI=10.1073/pnas.1512947113;
RA Kilmury S.L., Burrows L.L.;
RT "Type IV pilins regulate their own expression via direct intramembrane
RT interactions with the sensor kinase PilS.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:6017-6022(2016).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31431558; DOI=10.1128/mbio.02880-18;
RA Nieto V., Kroken A.R., Grosser M.R., Smith B.E., Metruccio M.M.E.,
RA Hagan P., Hallsten M.E., Evans D.J., Fleiszig S.M.J.;
RT "Type IV Pili Can Mediate Bacterial Motility within Epithelial Cells.";
RL MBio 10:0-0(2019).
CC -!- FUNCTION: Major 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:9282737, PubMed:26041805, PubMed:31431558). In addition,
CC plays a critical role in type II secretion of exoenzymes by interacting
CC with specific components such as XcpT or XcpU (PubMed:9282737).
CC Modulates host calcium signaling through interaction with host calcium-
CC modulating cyclophilin ligand (PubMed:23266901).
CC {ECO:0000269|PubMed:23266901, ECO:0000269|PubMed:26041805,
CC ECO:0000269|PubMed:31431558, ECO:0000269|PubMed:9282737}.
CC -!- SUBUNIT: Interacts with PilJ (PubMed:26041805). Interacts with PilS at
CC the inner membrane (PubMed:27162347). Interacts with type II secretion
CC system (T2SS) components XcpT, XcpU and XcpW (PubMed:9282737).
CC {ECO:0000269|PubMed:26041805, ECO:0000269|PubMed:27162347,
CC ECO:0000269|PubMed:9282737}.
CC -!- SUBCELLULAR LOCATION: Fimbrium. Cell inner membrane
CC {ECO:0000269|PubMed:27162347}; Single-pass membrane protein
CC {ECO:0000255}. Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23266901}.
CC -!- PTM: Methylated by prepilin peptidase PilD at the amino group of the N-
CC terminal phenylalanine once the leader sequence is cleaved.
CC {ECO:0000269|PubMed:1429457}.
CC -!- DISRUPTION PHENOTYPE: Mutants show a significant reduction in the
CC efficiency of extracellular protein secretion (PubMed:9282737). They
CC are also defective in twitching motility (PubMed:31431558).
CC {ECO:0000269|PubMed:31431558, ECO:0000269|PubMed:9282737}.
CC -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
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DR EMBL; M11323; AAA25954.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07913.1; -; Genomic_DNA.
DR PIR; A25023; A25023.
DR RefSeq; NP_253215.1; NC_002516.2.
DR RefSeq; WP_003112842.1; NZ_QZGE01000004.1.
DR PDB; 1PAN; NMR; -; A=133-149.
DR PDB; 1PAO; NMR; -; A=133-149.
DR PDBsum; 1PAN; -.
DR PDBsum; 1PAO; -.
DR AlphaFoldDB; P04739; -.
DR SMR; P04739; -.
DR STRING; 208964.PA4525; -.
DR TCDB; 3.A.15.2.1; the outer membrane protein secreting main terminal branch (mtb) family.
DR iPTMnet; P04739; -.
DR PaxDb; P04739; -.
DR PRIDE; P04739; -.
DR DNASU; 878423; -.
DR EnsemblBacteria; AAG07913; AAG07913; PA4525.
DR GeneID; 878423; -.
DR KEGG; pae:PA4525; -.
DR PATRIC; fig|208964.12.peg.4736; -.
DR PseudoCAP; PA4525; -.
DR HOGENOM; CLU_091705_4_2_6; -.
DR OMA; ATAHCAI; -.
DR PhylomeDB; P04739; -.
DR BioCyc; PAER208964:G1FZ6-4615-MON; -.
DR EvolutionaryTrace; P04739; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:CACAO.
DR GO; GO:0005829; C:cytosol; IDA:CACAO.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009289; C:pilus; IDA:PseudoCAP.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044096; C:type IV pilus; IDA:PseudoCAP.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:PseudoCAP.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IMP:PseudoCAP.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:PseudoCAP.
DR GO; GO:0043683; P:type IV pilus assembly; IBA:GO_Central.
DR GO; GO:0043107; P:type IV pilus-dependent motility; IDA:PseudoCAP.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR001082; Pilin.
DR InterPro; IPR045584; Pilin-like.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF00114; Pilin; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Disulfide bond; Fimbrium;
KW Host endoplasmic reticulum; Host membrane; Membrane; Methylation;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT PROPEP 1..6
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:1429457"
FT /id="PRO_0000024178"
FT CHAIN 7..149
FT /note="Type IV major pilin protein PilA"
FT /id="PRO_0000024179"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:8330261"
FT DISULFID 134..147
FT MUTAGEN 7
FT /note="F->C: Loss of processing by PilD."
FT /evidence="ECO:0000269|PubMed:1429457"
FT MUTAGEN 11
FT /note="E->A: Decrease in methylation of F-7 and loss of
FT pili assembly."
FT /evidence="ECO:0000269|PubMed:8330261"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1PAN"
SQ SEQUENCE 149 AA; 15512 MW; 98EC8A6F7B022214 CRC64;
MKAQKGFTLI ELMIVVAIIG ILAAIAIPQY QNYVARSEGA SALATINPLK TTVEESLSRG
IAGSKIKIGT TASTATETYV GVEPDANKLG VIAVAIEDSG AGDITFTFQT GTSSPKNATK
VITLNRTADG VWACKSTQDP MFTPKGCDN
