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Fap1 adhesin (Fimbriae-associated protein Fap1) (Serine-rich repeat protein Fap1)

 FAP1_STRPA              Reviewed;        2587 AA.
A1C3L3; Q9ZFF9;
25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 1.
28-FEB-2018, entry version 41.
RecName: Full=Fap1 adhesin;
AltName: Full=Fimbriae-associated protein Fap1;
AltName: Full=Serine-rich repeat protein Fap1;
Flags: Precursor;
Name=fap1;
Streptococcus parasanguinis.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=1318;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
DOMAIN, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=FW213;
PubMed=10594831; DOI=10.1046/j.1365-2958.1999.01670.x;
Wu H., Fives-Taylor P.M.;
"Identification of dipeptide repeats and a cell wall sorting signal in
the fimbriae-associated adhesin, Fap1, of Streptococcus parasanguis.";
Mol. Microbiol. 34:1070-1081(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, PARTIAL
EXPORT VIA THE ACCESSORY SECA2/SECY2 SYSTEM, AND GLYCOSYLATION.
STRAIN=FW213;
PubMed=16997950; DOI=10.1128/JB.00836-06;
Wu H., Bu S., Newell P., Chen Q., Fives-Taylor P.;
"Two gene determinants are differentially involved in the biogenesis
of Fap1 precursors in Streptococcus parasanguis.";
J. Bacteriol. 189:1390-1398(2007).
[3]
PROTEIN SEQUENCE OF 86-106, FUNCTION, SUBCELLULAR LOCATION, INDUCTION,
GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
STRAIN=FW213;
PubMed=9632253; DOI=10.1046/j.1365-2958.1998.00805.x;
Wu H., Mintz K.P., Ladha M., Fives-Taylor P.M.;
"Isolation and characterization of Fap1, a fimbriae-associated adhesin
of Streptococcus parasanguis FW213.";
Mol. Microbiol. 28:487-500(1998).
[4]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 191-513, STRUCTURE BY NMR OF
213-93, AND MUTAGENESIS OF ILE-219; GLU-223; ASP-227; LEU-248;
VAL-249; GLU-289; 376-ILE-LEU-377; LEU-385; LEU-470; ASN-488; GLN-490
AND ILE-496.
STRAIN=FW213;
PubMed=20584910; DOI=10.1074/jbc.M110.128165;
Ramboarina S., Garnett J.A., Zhou M., Li Y., Peng Z., Taylor J.D.,
Lee W.C., Bodey A., Murray J.W., Alguel Y., Bergeron J., Bardiaux B.,
Sawyer E., Isaacson R., Tagliaferri C., Cota E., Nilges M.,
Simpson P., Ruiz T., Wu H., Matthews S.;
"Structural insights into serine-rich fimbriae from gram-positive
bacteria.";
J. Biol. Chem. 285:32446-32457(2010).
-!- FUNCTION: The major structural element of fimbriae. Required for
adherence to saliva-coated hydroxyapatite beads (SHA), an in vitro
tooth model. A Fap1-dependent increase in adherence is seen as the
pH is reduced from pH 8 to pH 5. {ECO:0000269|PubMed:10594831,
ECO:0000269|PubMed:9632253}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Secreted, cell wall;
Peptidoglycan-anchor. Fimbrium. Note=Primarily but not exclusively
exported by the accessory SecA2/SecY2 protein translocation
apparatus.
-!- INDUCTION: Low expression in early log phase, it increases until
stationary phase (at protein level). A monocistronic transcript.
{ECO:0000269|PubMed:10594831, ECO:0000269|PubMed:9632253}.
-!- DOMAIN: Has short and long regions consisting of (E/V/I)S
dipeptide repeats. These Ser-rich regions have 28 and 1000 repeats
respectively. {ECO:0000269|PubMed:10594831}.
-!- PTM: Glycosylated; occurs within the cytoplasm.
{ECO:0000269|PubMed:16997950, ECO:0000269|PubMed:9632253}.
-!- DISRUPTION PHENOTYPE: Loss of fimbriae on the cell surface, loss
of adherence to saliva-coated hydroxyapatite beads (SAH), an in
vitro tooth model. {ECO:0000269|PubMed:10594831,
ECO:0000269|PubMed:9632253}.
-!- SIMILARITY: Belongs to the SraP family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-18 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC79868.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF100426; AAC79868.1; ALT_INIT; Genomic_DNA.
EMBL; DQ990875; ABL73998.1; -; Genomic_DNA.
PIR; T17451; T17451.
PDB; 2KUB; NMR; -; A=213-293.
PDB; 2X12; X-ray; 2.90 A; A/B=191-522.
PDB; 3RGU; X-ray; 3.00 A; A/B/C/D=201-316.
PDBsum; 2KUB; -.
PDBsum; 2X12; -.
PDBsum; 3RGU; -.
SMR; A1C3L3; -.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
InterPro; IPR007383; DUF445.
InterPro; IPR019948; Gram-positive_anchor.
InterPro; IPR022263; KxYKxGKxW.
InterPro; IPR026465; Ser_adhes_glycop.
Pfam; PF04286; DUF445; 1.
Pfam; PF00746; Gram_pos_anchor; 1.
TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
TIGRFAMs; TIGR04224; ser_adhes_Nterm; 1.
PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
1: Evidence at protein level;
3D-structure; Cell wall; Cytoplasm; Direct protein sequencing;
Fimbrium; Peptidoglycan-anchor; Secreted; Signal.
SIGNAL 1 85 {ECO:0000269|PubMed:9632253}.
CHAIN 86 2554 Fap1 adhesin.
/FTId=PRO_0000414882.
PROPEP 2555 2587 Removed by sortase. {ECO:0000255|PROSITE-
ProRule:PRU00477}.
/FTId=PRO_0000414883.
REGION 107 195 Ser-rich region 1.
REGION 191 522 Sufficient to block adherence to beads.
REGION 516 2561 Ser-rich region 2.
REGION 2367 2587 Required for localization to cell wall,
fimbriae formation and adherence to
saliva-coated hydroxyapatite beads (SHA)
but not secretion.
MOTIF 2551 2555 LPXTG sorting signal.
{ECO:0000255|PROSITE-ProRule:PRU00477}.
COMPBIAS 107 195 Ser-rich.
COMPBIAS 516 2561 Ser-rich.
COMPBIAS 540 2548 Glu-rich.
COMPBIAS 550 2510 Val-rich.
MOD_RES 2554 2554 Pentaglycyl murein peptidoglycan amidated
threonine. {ECO:0000255|PROSITE-
ProRule:PRU00477}.
MUTAGEN 219 219 I->A: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 223 223 E->A: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 227 227 D->A: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 248 248 L->A: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 249 249 V->A: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 289 289 E->A: Adheres to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 376 377 IL->AA: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 385 385 L->A: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 470 470 L->A: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 488 488 N->A: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 490 490 Q->A: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
MUTAGEN 496 496 I->A: Loss of adherence to SHA.
{ECO:0000269|PubMed:20584910}.
CONFLICT 461 461 K -> E (in Ref. 1; AAC79868).
{ECO:0000305}.
CONFLICT 528 528 T -> A (in Ref. 1; AAC79868).
{ECO:0000305}.
CONFLICT 1146 1146 V -> P (in Ref. 1; AAC79868).
{ECO:0000305}.
CONFLICT 1226 1226 I -> S (in Ref. 1; AAC79868).
{ECO:0000305}.
CONFLICT 1830 1830 V -> M (in Ref. 1; AAC79868).
{ECO:0000305}.
CONFLICT 1861 1861 S -> P (in Ref. 1; AAC79868).
{ECO:0000305}.
CONFLICT 1885 1885 S -> T (in Ref. 1; AAC79868).
{ECO:0000305}.
HELIX 216 234 {ECO:0000244|PDB:3RGU}.
HELIX 238 263 {ECO:0000244|PDB:3RGU}.
STRAND 264 267 {ECO:0000244|PDB:3RGU}.
HELIX 269 293 {ECO:0000244|PDB:3RGU}.
STRAND 322 326 {ECO:0000244|PDB:2X12}.
HELIX 327 329 {ECO:0000244|PDB:2X12}.
TURN 330 332 {ECO:0000244|PDB:2X12}.
STRAND 336 339 {ECO:0000244|PDB:2X12}.
STRAND 351 359 {ECO:0000244|PDB:2X12}.
TURN 360 362 {ECO:0000244|PDB:2X12}.
STRAND 364 371 {ECO:0000244|PDB:2X12}.
TURN 373 377 {ECO:0000244|PDB:2X12}.
HELIX 380 382 {ECO:0000244|PDB:2X12}.
STRAND 386 394 {ECO:0000244|PDB:2X12}.
STRAND 399 409 {ECO:0000244|PDB:2X12}.
STRAND 414 417 {ECO:0000244|PDB:2X12}.
STRAND 427 434 {ECO:0000244|PDB:2X12}.
STRAND 436 438 {ECO:0000244|PDB:2X12}.
STRAND 442 450 {ECO:0000244|PDB:2X12}.
HELIX 454 459 {ECO:0000244|PDB:2X12}.
STRAND 461 471 {ECO:0000244|PDB:2X12}.
STRAND 481 485 {ECO:0000244|PDB:2X12}.
STRAND 487 490 {ECO:0000244|PDB:2X12}.
STRAND 492 496 {ECO:0000244|PDB:2X12}.
STRAND 498 510 {ECO:0000244|PDB:2X12}.
TURN 514 516 {ECO:0000244|PDB:2X12}.
SEQUENCE 2587 AA; 265063 MW; C8AD6E9F6EE8FE5A CRC64;
MGKYKRAGET SRKTRVKMHK SGKNWVRTLI SQIGLMHFLG GSISEKKINV DVYEQKNISA
STILKGAVAL GALTGATVVS GNVFADETVL AKETTLTTTD ANEVKLSSEN FDSEKAEEKI
SLSQSESASE SVSESISESV SESVSTSESV SESVSESVSE SISESVSESI SESISESVSE
STSTSIVLSE SGAASGNKAT SKGTEEKQDS VRENLDKMIS EAEVLNDMAA RKLITLDAEQ
QLELMKSLVA TQSQLEATKN LIGDPNATVA DLQIAYTTLG NNTQALGNEL IKLNPNGQIY
AVLNNTEASR AATLRSTTTG TKTTFTISDF SNGGTQYYWA GGNANNLKNP ISSISAVYDS
ATGKISWTVE YDPTTILKSP ALKTLKTYTG IYIDTSSDSK LSTPTNVLID GAATNPVTNF
YGNGSKGIEY VSKGTTKGVT KHTITFDTAF SGRANDLADL KIKMLAATTL SDPHFYEDGS
KGNYGRYNGQ TAPYVIANDS GTAIGGYQVS GVNADSIPSD TTSQSESTSK SESTSKSISE
SVIESISESV IGSVSESVSE SVSESVSESI TESVSESVSE SISESVSESV SESISESVSE
SVSESISESV SESVSESISE SVSESVSESI SESISESVSE SVSESISESV SESVSESISE
SVSESVSESI SESVSESVSE SISESVSESV SESISESVSE SVSESISESV SESVSESISE
SVSESVSESI SESVSESVSE SISESVSESV SESISESVSE SVSESISESV SESVSESVSE
SVSESVSESI SESVSESVSE SVSESVSESV SESVSESISE SVSESVSESI SESVSESVSE
SISESVSESV SESISESVSE SVSESISESV SESVSESISE SVSESVSESI SESVSESVSE
SISESVSESV SESISESVSE SVSESISESV SESVSESVSE SVSESVSESV SESVSESISE
SVSESVSESI SESVSESVSE SISESVSESV SESISESVSE SVSESISESV SESVSESVSE
SVSESVSESV SESVSESISE SVSESVSESV SESISESVSE SVSESISESV SESVSESISE
SVSESVSESV SESVSESVSE SISESVSESV SESISESVSE SVSESISESV SESVSESISE
SVSESVSESI SESVSESVSE SISESVSESV SESVSESVSE SVSESISESV SESVSESISE
SVSESVSESV SESISESVSE SVSESISESV SESVSESISE SVSESVSESI SESVSESVSE
SVSESVSESV SESVSESVSE SVSESVSESI SESVSESVSE SVSESISESV SESVSESISE
SVSESVSESI SESVSESVSE SISESVSESV SESISESVSE SVSESISESV SESVSESVSE
SVSESVSESI SESVSESVSE SISESVSESV SESISESVSE SVSESISESV SESVSESVSE
SISESVSESV SESISESVSE SVSESISESV SESVSESVSE SVSESVSESV SESVSESVSE
SISESVSESV SESISESVSE SVSESISESV SESVSESISE SVSESVSESI SESVSESVSE
SISESVSESV SESISESVSE SVSESVSESV SESVSESISE SVSESVSESI SESVSESVSE
SVSESVSESV SESVSESVSE SVSESISESV SESVSESVSE SVSESVSESI SESVSESVSE
SISESVSESV SESISESVSE SVSESISESV SESVSESISE SVSESVSESI SESVSESVSE
SISESVSESV SESVSESVSE SVSESVSESV SESISESVSE SVSESISESV SESVSESISE
SVSESVSESV SESVSESVSE SISESVSESV SESISESVSE SVSESISESV SESVSESISE
SVSESVSESV SESISESVSE SVSESISESV SESVSESISE SVSESVSESI SESVSESVSE
SISESVSESV SESISESVSE SVSESVSESV SESVSESISE SVSESISESV SESVSESISE
SVSESVSESI SESVSESVSE SISESVSESV SESISESVSE SVSESISESV SESVSESISE
SVSESVSESI SESVSESVSE SVSESISESV SESVSESISE SVSESVSESI SESVSESVSE
SVSESVSESV SESVSESVSE SVSESISESV SESVSESISE SVSESVSESI SESVSESVSE
SISESVSESV SESISESVSE SVSESISESV SESVSESISE SVSESVSESV SESVSESVSE
SISESVSESV SESVSESISE SVSESVSESI SESVSESVSE SVSESVSESV SESVSESVSE
SVSESISESV SESVSESVSE SVSESVSESI SESVSESVSE SISESVSESV SESISESVSE
SVSESISESV SESVSESISE SVSESVSESI SESVSESVSE SISESVSESV SESISESVSE
SVSESVSESI SESVSESVSE SISESVSESV SESISESVSE SVSESISESV SESVSESVSE
SVSESVSESV SESVSESISE SVSESVSESI SESVSESVSE SVSESVSESV SESISESVSE
SISESVSESV SESISESVSE SVSESISERT LPNTGENVSS SLGLVGLSGL LFGALLGRKK
RKSEDAE


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