PILY1_PSEAW
ID PILY1_PSEAW Reviewed; 1163 AA.
AC S0HPF7; A8WE64;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Type IV pilus biogenesis factor PilY1 {ECO:0000303|PubMed:20080557};
DE AltName: Full=Pilus-associated adhesin PilY {ECO:0000303|PubMed:20331639};
DE Flags: Precursor;
GN Name=pilY1 {ECO:0000312|EMBL:ABW89597.1};
GN ORFNames=PAK_05020 {ECO:0000312|EMBL:EOT10199.1},
GN Y880_0129235 {ECO:0000312|EMBL:KAJ87266.1};
OS Pseudomonas aeruginosa (strain PAK).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1009714;
RN [1] {ECO:0000312|EMBL:ABW89597.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS)
RP OF 615-1163 OF LEU-712/812/823-MET MUTANT IN COMPLEX WITH CALCIUM,
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP ASP-859, AND CIRCULAR DICHROISM.
RC STRAIN=PAK {ECO:0000312|EMBL:ABW89597.1};
RX PubMed=20080557; DOI=10.1073/pnas.0911616107;
RA Orans J., Johnson M.D., Coggan K.A., Sperlazza J.R., Heiniger R.W.,
RA Wolfgang M.C., Redinbo M.R.;
RT "Crystal structure analysis reveals Pseudomonas PilY1 as an essential
RT calcium-dependent regulator of bacterial surface motility.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1065-1070(2010).
RN [2] {ECO:0000312|EMBL:EOT10199.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAK {ECO:0000312|EMBL:EOT10199.1};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Hung D., Lory S., Poulsen B., Penaranda C., Ausubel F., Walker B.,
RA Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Pseudomonas aeruginosa PAK.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:KAJ87266.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAK {ECO:0000312|EMBL:KAJ87266.1};
RA Jorth P., Whiteley M.;
RT "Draft genome sequence of Pseudomonas aeruginosa PAK.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAK {ECO:0000303|PubMed:8899718};
RX PubMed=8899718; DOI=10.1111/j.1365-2958.1996.tb02665.x;
RA Alm R.A., Hallinan J.P., Watson A.A., Mattick J.S.;
RT "Fimbrial biogenesis genes of Pseudomonas aeruginosa: pilW and pilX
RT increase the similarity of type 4 fimbriae to the GSP protein-secretion
RT systems and pilY1 encodes a gonococcal PilC homologue.";
RL Mol. Microbiol. 22:161-173(1996).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAK {ECO:0000303|PubMed:20331639};
RX PubMed=20331639; DOI=10.1111/j.1462-5822.2010.01461.x;
RA Heiniger R.W., Winther-Larsen H.C., Pickles R.J., Koomey M., Wolfgang M.C.;
RT "Infection of human mucosal tissue by Pseudomonas aeruginosa requires
RT sequential and mutually dependent virulence factors and a novel pilus-
RT associated adhesin.";
RL Cell. Microbiol. 12:1158-1173(2010).
RN [6]
RP FUNCTION, INTERACTION WITH HOST INTEGRINS, CALCIUM-BINDING, CIRCULAR
RP DICHROISM, AND MUTAGENESIS OF ASP-600.
RX PubMed=22242136; DOI=10.1371/journal.pone.0029629;
RA Johnson M.D., Garrett C.K., Bond J.E., Coggan K.A., Wolfgang M.C.,
RA Redinbo M.R.;
RT "Pseudomonas aeruginosa PilY1 binds integrin in an RGD- and calcium-
RT dependent manner.";
RL PLoS ONE 6:E29629-E29629(2011).
CC -!- FUNCTION: Involved in pilus assembly, twitching motility and adhesion
CC to host cells. Primes type IV pili (T4P) assembly and is required for
CC inclusion of minor pilins PilV, PilW and PilX to the surface pili (By
CC similarity). Stabilizes assembled pilus fibers likely by antagonizing
CC retraction mediated by PilT. Calcium-binding and calcium release by
CC PilY1 seem to be essential for twitching motility and for regulation of
CC pilus retraction dynamics of PilT. Adhesin for human tissue
CC specifically recognizing a host receptor localized or enriched on
CC basolateral epithelial cell surfaces. Binds host integrins in an
CC calcium-dependent manner in vitro and this interaction may be employed
CC by the bacterium to mediate host epithelial cell binding in vivo.
CC {ECO:0000250|UniProtKB:Q9HVM8, ECO:0000269|PubMed:20080557,
CC ECO:0000269|PubMed:20331639, ECO:0000269|PubMed:22242136}.
CC -!- SUBUNIT: Interacts (via C-terminal 532-1163) with host integrins alpha-
CC V/beta-3 (ITGAV/ITGB3) and alpha-V/beta-5 (ITGAV/ITGB5).
CC {ECO:0000269|PubMed:22242136}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:20080557}. Membrane
CC {ECO:0000269|PubMed:8899718}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q02GC2}. Note=Colocalizes with the T4P fraction
CC when surface pili are present (PubMed:20331639, PubMed:8899718).
CC Sheared surface fraction when PilV, PilW and PilX are also present (By
CC similarity). {ECO:0000250|UniProtKB:Q9HVM8,
CC ECO:0000269|PubMed:20331639, ECO:0000269|PubMed:8899718}.
CC -!- DISRUPTION PHENOTYPE: Loss of surface T4P which is not due to the lack
CC of major pilus structural subunit PilA (PubMed:20080557,
CC PubMed:8899718, PubMed:20331639). Lacks measurable twitching motility
CC (PubMed:20080557, PubMed:8899718). T4P fibers are restored when pilus
CC retraction ATPase pilT is deleted at the same time. Does not bind to
CC the injured regions of human ciliated airway epithelium (HAE) during
CC bacterial infection on the contrary to the wild-type which
CC preferentially binds to the injured regions of the HAE
CC (PubMed:20331639). {ECO:0000269|PubMed:20080557,
CC ECO:0000269|PubMed:20331639, ECO:0000269|PubMed:8899718}.
CC -!- MISCELLANEOUS: Residues 600-608 comprise a calcium-binding site which
CC together with the other one (residues 851-859) seems important for
CC interaction with integrins of the host. {ECO:0000269|PubMed:22242136}.
CC -!- SIMILARITY: Belongs to the PilY1 family. {ECO:0000305}.
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DR EMBL; EU234515; ABW89597.1; -; Genomic_DNA.
DR EMBL; ASWU01000022; EOT10199.1; -; Genomic_DNA.
DR EMBL; AZUG01000415; KAJ87266.1; -; Genomic_DNA.
DR RefSeq; WP_010793785.1; NZ_LR657304.1.
DR PDB; 3HX6; X-ray; 2.10 A; A/B=615-1163.
DR PDBsum; 3HX6; -.
DR AlphaFoldDB; S0HPF7; -.
DR SMR; S0HPF7; -.
DR PATRIC; fig|1009714.6.peg.5062; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0044096; C:type IV pilus; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0043683; P:type IV pilus assembly; IMP:UniProtKB.
DR GO; GO:0043107; P:type IV pilus-dependent motility; IMP:UniProtKB.
DR InterPro; IPR008707; PilC_beta_prop_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR Pfam; PF05567; Neisseria_PilC; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Fimbrium; Fimbrium biogenesis; Membrane;
KW Metal-binding; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000312|EMBL:ABW89597.1"
FT CHAIN 31..1163
FT /note="Type IV pilus biogenesis factor PilY1"
FT /evidence="ECO:0000312|EMBL:ABW89597.1"
FT /id="PRO_0000431917"
FT REGION 329..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..621
FT /note="Integrin-binding motif RGD"
FT /evidence="ECO:0000303|PubMed:22242136"
FT REGION 1138..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:22242136"
FT BINDING 602
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:22242136"
FT BINDING 604
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:22242136"
FT BINDING 608
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:22242136"
FT BINDING 851
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20080557"
FT BINDING 853
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20080557"
FT BINDING 855
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20080557"
FT BINDING 857
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20080557"
FT BINDING 859
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20080557"
FT MUTAGEN 600
FT /note="D->A: Abolishes integrin binding and calcium binding
FT in the first site."
FT /evidence="ECO:0000269|PubMed:22242136"
FT MUTAGEN 600
FT /note="D->K: Preserves integrin binding."
FT /evidence="ECO:0000269|PubMed:22242136"
FT MUTAGEN 859
FT /note="D->A: Loss of calcium-binding. Significantly reduced
FT twitching motility. Dramatically reduced level of surface
FT T4P. Regains ability to produce normal levels of T4P and is
FT capable of trafficking to the T4P fraction; when associated
FT with pilT deletion mutant."
FT /evidence="ECO:0000269|PubMed:20080557"
FT MUTAGEN 859
FT /note="D->K: Loss of calcium-binding. Significantly reduced
FT twitching motility. Insensitive to the effects of calcium
FT chelator EGTA and produces an abundance of non-functional
FT surface T4P. Capable of trafficking to the T4P fraction."
FT /evidence="ECO:0000269|PubMed:20080557"
SQ SEQUENCE 1163 AA; 126248 MW; 7FCED3BE18D5FC52 CRC64;
MKSALHQIGK TSLAAALSGA VLLSAQTTHA AALSVSQQPL MLIQGVAPNM LVTLDDSGSM
AYAYAPDSLV NSRNNVYFAS NSYNPMYFDP NTQYKLPKKV TLSNGQIQVQ DYSKPSFTAA
WRNGFTQEGR VNLSRDYRPT VQYQGGSGAG TESSIDWYGA PAFYYQYSGG RGCSLTTSSC
YTRVEISGAA QQQNFANWYS FYRTRALATQ TAANLAFYSL PENARISWQL LNSSSCLIGS
GSSNCYNNYL RDFTGQHRVN FFNWLENLSV GGGTPLRQAM TRAGEFLKKT GVNGPYAYRP
GTQTSPEYSC RGSYHILMTD GLWNNDSASV GNADSTSRSL PDGKSYSSQT PYRDAASNTL
ADQAFHYWAT DARPDIDDNI KPYIPYPDQA NPSAEYWNPR NDPATWQHMV TYTLGLGLTT
SLTSPKWEGS TYSGGYDEIA AGRLSWPNAS NNHSNNVYDL WHAAVNSRGE FFSADSPDQL
VAAFQDILNR ISGKDLPASR PAISSSLQED DTGDKLTRFA YQTSFASDKN WAGDLTRYSL
TTQDKATVQT KLWSAQSILD AMPNGGAGRK IMMAGSGTSG LKEFTWGSLS ADQQRQLNRD
PDRNDVADTK GQDRVAFLRG DRSKENSDNF RTRNSILGDI INSSPATVGK AQYLTYLAQP
IEPSGNYSTF AEAQKTRAPR VYVGANDGML HGFDTDGNET FAFIPSAVFE KLHKLTARGY
QGGAHQFYVD GSPVVADAFF GGAWHTVLIG SLRAGGKGLF ALDVTDPANI KLLWEIGVDQ
EPDLGYSFPK PTVARLHNGK WAVVTGNGYS SLNDKAALLI IDLETGAITR KLEVTGRTGV
PNGLSSPRLA DNNSDGVADY AYAGDLQGNL WRFDLIAGKV NQDDPFSRAN DGPAVASSFR
VSFGGQPLYS AVDSAGAAQA ITAAPSLVRH PTRKGYIVIF GTGKYFENAD ARADTSRAQT
LYGIWDQQTK GEAAGSTPRL TRGNLQQQTL DLQADSTFAS TARTIRIASQ NPVNWLNNDG
STKQSGWYLD FMVNGTLKGE MLIEDMIAIG QVVLLQTITP NDDPCADGAS NWTYGLDPYT
GGRTSFTVFD LARQGVVDSK SDYSYNKQNV AVSGTEQKGL GGLTLSTNEQ GNPEVCSSGE
CLTVNPGPNT RGRQNWRPIE GKN
