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Type IV pilus biogenesis factor PilY1 (Pilus-associated adhesin PilY1)

 PILY1_PSEAE             Reviewed;        1161 AA.
Q9HVM8; Q51536;
04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
07-NOV-2018, entry version 89.
RecName: Full=Type IV pilus biogenesis factor PilY1 {ECO:0000250|UniProtKB:S0HPF7};
AltName: Full=Pilus-associated adhesin PilY1 {ECO:0000303|PubMed:25389296};
Flags: Precursor;
Name=pilY1 {ECO:0000312|EMBL:AAA93502.1, ECO:0000312|EMBL:AAG07942.1};
OrderedLocusNames=PA4554 {ECO:0000312|EMBL:AAG07942.1};
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=208964 {ECO:0000312|EMBL:AAG07942.1};
[1] {ECO:0000312|PIR:S72645}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1 {ECO:0000303|PubMed:8899718};
PubMed=8899718; DOI=10.1111/j.1365-2958.1996.tb02665.x;
Alm R.A., Hallinan J.P., Watson A.A., Mattick J.S.;
"Fimbrial biogenesis genes of Pseudomonas aeruginosa: pilW and pilX
increase the similarity of type 4 fimbriae to the GSP protein-
secretion systems and pilY1 encodes a gonococcal PilC homologue.";
Mol. Microbiol. 22:161-173(1996).
[2] {ECO:0000312|EMBL:AAG07942.1, ECO:0000312|Proteomes:UP000002438}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1 {ECO:0000312|Proteomes:UP000002438};
PubMed=10984043; DOI=10.1038/35023079;
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an
opportunistic pathogen.";
Nature 406:959-964(2000).
[3]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=25389296; DOI=10.1074/jbc.M114.616904;
Nguyen Y., Sugiman-Marangos S., Harvey H., Bell S.D., Charlton C.L.,
Junop M.S., Burrows L.L.;
"Pseudomonas aeruginosa minor pilins prime type IVa pilus assembly and
promote surface display of the PilY1 adhesin.";
J. Biol. Chem. 290:601-611(2015).
-!- FUNCTION: Involved in pilus assembly, twitching motility and
adhesion to host cells. Primes type IV pili (T4P) assembly and is
required for inclusion of minor pilins PilV, PilW and PilX to the
surface pili (PubMed:25389296). Stabilizes assembled pilus fibers
likely by antagonizing retraction mediated by PilT. Calcium-
binding and calcium release by PilY1 seem to be essential for
twitching motility and for regulation of pilus retraction dynamics
of PilT (By similarity). {ECO:0000250|UniProtKB:S0HPF7,
ECO:0000269|PubMed:25389296}.
-!- SUBUNIT: Interacts (via C-terminus) with host integrins alpha-
V/beta-3 (ITGAV/ITGB3) and alpha-V/beta-5 (ITGAV/ITGB5).
{ECO:0000250|UniProtKB:S0HPF7}.
-!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250|UniProtKB:S0HPF7}.
Membrane {ECO:0000250|UniProtKB:S0HPF7}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q02GC2}. Note=Colocalizes with the T4P
fraction when surface pili are present (By similarity). Sheared
surface fraction when PilV, PilW and PilX are also present
(PubMed:25389296). {ECO:0000250|UniProtKB:S0HPF7,
ECO:0000269|PubMed:25389296}.
-!- DISRUPTION PHENOTYPE: Pilus assembly severely impaired.
Retraction-deficient. Prevents incorporation of PilE into pili.
{ECO:0000269|PubMed:25389296}.
-!- MISCELLANEOUS: Residues 598-606 comprise a calcium-binding site
which together with the other one (residues 849-857) seems
important for interaction with integrins of the host.
{ECO:0000250|UniProtKB:S0HPF7}.
-!- SIMILARITY: Belongs to the PilY1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA93502.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAA93502.1; Type=Frameshift; Positions=239, 273, 281, 1096, 1101, 1106, 1111; Evidence={ECO:0000305};
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EMBL; L76605; AAA93502.1; ALT_SEQ; Genomic_DNA.
EMBL; AE004091; AAG07942.1; -; Genomic_DNA.
PIR; D83076; D83076.
PIR; S72645; S72645.
RefSeq; NP_253244.1; NC_002516.2.
RefSeq; WP_003115287.1; NC_002516.2.
ProteinModelPortal; Q9HVM8; -.
SMR; Q9HVM8; -.
STRING; 208964.PA4554; -.
TCDB; 9.A.21.1.2; the comc dna uptake competence (comc) family.
PaxDb; Q9HVM8; -.
PRIDE; Q9HVM8; -.
EnsemblBacteria; AAG07942; AAG07942; PA4554.
GeneID; 877859; -.
KEGG; pae:PA4554; -.
PATRIC; fig|208964.12.peg.4766; -.
PseudoCAP; PA4554; -.
eggNOG; ENOG4105CWU; Bacteria.
eggNOG; COG3419; LUCA.
HOGENOM; HOG000271874; -.
InParanoid; Q9HVM8; -.
KO; K02674; -.
OMA; LWHAAVN; -.
PhylomeDB; Q9HVM8; -.
BioCyc; PAER208964:G1FZ6-4647-MONOMER; -.
Proteomes; UP000002438; Chromosome.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0043107; P:type IV pilus-dependent motility; IMP:PseudoCAP.
InterPro; IPR008707; PilC_beta_prop_dom.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
Pfam; PF05567; Neisseria_PilC; 1.
SUPFAM; SSF50998; SSF50998; 1.
3: Inferred from homology;
Calcium; Complete proteome; Cytoplasm; Fimbrium; Fimbrium biogenesis;
Membrane; Metal-binding; Reference proteome; Signal.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 1161 Type IV pilus biogenesis factor PilY1.
{ECO:0000255}.
/FTId=PRO_0000431916.
REGION 598 606 Calcium-binding.
{ECO:0000250|UniProtKB:S0HPF7}.
REGION 617 619 Integrin-binding motif RGD.
{ECO:0000250|UniProtKB:S0HPF7}.
METAL 849 849 Calcium. {ECO:0000250|UniProtKB:S0HPF7}.
METAL 851 851 Calcium. {ECO:0000250|UniProtKB:S0HPF7}.
METAL 853 853 Calcium. {ECO:0000250|UniProtKB:S0HPF7}.
METAL 855 855 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:S0HPF7}.
METAL 857 857 Calcium. {ECO:0000250|UniProtKB:S0HPF7}.
CONFLICT 128 128 S -> R (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 169 169 C -> W (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 203 203 A -> R (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 213 214 YS -> FR (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 239 239 S -> G (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 255 255 H -> Q (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 273 273 P -> H (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 281 281 A -> G (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 388 388 A -> D (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 392 392 A -> G (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 403 403 T -> I (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 417 417 T -> N (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 549 549 K -> N (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 594 594 Q -> K (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 845 845 P -> L (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 892 892 A -> T (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 1006 1006 A -> G (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 1083 1083 S -> R (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 1090 1090 A -> G (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 1102 1102 S -> R (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 1106 1106 Q -> R (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 1109 1110 AV -> GN (in Ref. 1; AAA93502).
{ECO:0000305}.
CONFLICT 1129 1129 G -> A (in Ref. 1; AAA93502).
{ECO:0000305}.
SEQUENCE 1161 AA; 126584 MW; 027E092E1084141F CRC64;
MKSVLHQIGK TSLAAALSGA VLLSAQTTHA AALSVSQQPL MLIQGVAPNM LVTLDDSGSM
AFAYAPDSIS GYGNYTFFAS NSFNPMYFDP NTQYKLPKKL TLVNGQVQIQ DYPAPNFSSA
WRNGFTRSGS INLSNSYKVT IEYGRGYDKE STIKADAAYY YDFTGSSSCN RTNQACYTRR
YVSTEQRQNF ANWYSFYRTR ALATQTAANL AFYSLPENAR VSWQLLNDSN CNQMGSGSSS
GNCFSNYLRD FTGQHRVNFF NWLEKLSVNG GTPLRQAMTR AGEFLKKTGV NGPYAYRPGT
QTAPEYSCRG SYHILMTDGL WNNDSANVGN ADSTARNLPD GKSYSSQTPY RDGTFDTLAD
QAFHYWATDA RPDIDDNIKP YIPYPDQANP SAEYWNPRND PATWQHMVTY TLGLGLTTSL
TSPRWEGSTF SGGYNDIVAG NLSWPRASNN DSNNVYDLWH AAVNSRGEFF SADSPDQLVA
AFQDILNRIS GKDLPASRPA ISSSLQEDDT GDKLTRFAYQ TSFASDKNWA GDLTRYSLTT
QDKATVQTKL WSAQSILDAM PNGGAGRKIM MAGSGTSGLK EFTWGSLSAD QQRQLNRDPD
RNDVADTKGQ DRVAFLRGDR RKENSDNFRT RNSILGDIIN SSPATVGKAQ YLTYLAQPIE
PSGNYSTFAE AQKTRAPRVY VGANDGMLHG FDTDGNETFA FIPSAVFEKL HKLTARGYQG
GAHQFYVDGS PVVADAFFGG AWHTVLIGSL RAGGKGLFAL DVTDPANIKL LWEIGVDQEP
DLGYSFPKPT VARLHNGKWA VVTGNGYSSL NDKAALLIID LETGAITRKL EVTGRTGVPN
GLSSPRLADN NSDGVADYAY AGDLQGNLWR FDLIAGKVNQ DDPFSRANDG PAVASSFRVS
FGGQPLYSAV DSAGAAQAIT AAPSLVRHPT RKGYIVIFGT GKYFENADAR ADTSRAQTLY
GIWDQQTKGE AAGSTPRLTR GNLQQQTLDL QADSTFASTA RTIRIASQNP VNWLNNDGST
KQSGWYLDFM VNGTLKGEML IEDMIAIGQV VLLQTITPND DPCADGASNW TYGLDPYTGG
RTSFTVFDLA RQGVVDSKSD YSYNKQNVAV SGTEQKGLGG LTLSTNEQGN PEVCSSGECL
TVNPGPNTRG RQNWRPIEGK N


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