FAP1_STRPA
ID FAP1_STRPA Reviewed; 2587 AA.
AC A1C3L3; Q9ZFF9;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Fap1 adhesin;
DE AltName: Full=Adhesin Fap1 {ECO:0000305};
DE AltName: Full=Fimbriae-associated protein Fap1;
DE AltName: Full=Serine-rich repeat protein Fap1;
DE Flags: Precursor;
GN Name=fap1;
OS Streptococcus parasanguinis.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1318;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, DOMAIN,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=FW213;
RX PubMed=10594831; DOI=10.1046/j.1365-2958.1999.01670.x;
RA Wu H., Fives-Taylor P.M.;
RT "Identification of dipeptide repeats and a cell wall sorting signal in the
RT fimbriae-associated adhesin, Fap1, of Streptococcus parasanguis.";
RL Mol. Microbiol. 34:1070-1081(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, PARTIAL EXPORT VIA
RP THE ACCESSORY SECA2/SECY2 SYSTEM, AND GLYCOSYLATION.
RC STRAIN=FW213;
RX PubMed=16997950; DOI=10.1128/jb.00836-06;
RA Wu H., Bu S., Newell P., Chen Q., Fives-Taylor P.;
RT "Two gene determinants are differentially involved in the biogenesis of
RT Fap1 precursors in Streptococcus parasanguis.";
RL J. Bacteriol. 189:1390-1398(2007).
RN [3]
RP PROTEIN SEQUENCE OF 86-106, FUNCTION, SUBCELLULAR LOCATION, INDUCTION,
RP GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=FW213;
RX PubMed=9632253; DOI=10.1046/j.1365-2958.1998.00805.x;
RA Wu H., Mintz K.P., Ladha M., Fives-Taylor P.M.;
RT "Isolation and characterization of Fap1, a fimbriae-associated adhesin of
RT Streptococcus parasanguis FW213.";
RL Mol. Microbiol. 28:487-500(1998).
RN [4]
RP GLYCOSYLATION.
RC STRAIN=FW213;
RX PubMed=20164186; DOI=10.1074/jbc.m109.066928;
RA Zhou M., Zhu F., Dong S., Pritchard D.G., Wu H.;
RT "A novel glucosyltransferase is required for glycosylation of a serine-rich
RT adhesin and biofilm formation by Streptococcus parasanguinis.";
RL J. Biol. Chem. 285:12140-12148(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 191-513, STRUCTURE BY NMR OF
RP 213-93, AND MUTAGENESIS OF ILE-219; GLU-223; ASP-227; LEU-248; VAL-249;
RP GLU-289; 376-ILE-LEU-377; LEU-385; LEU-470; ASN-488; GLN-490 AND ILE-496.
RC STRAIN=FW213;
RX PubMed=20584910; DOI=10.1074/jbc.m110.128165;
RA Ramboarina S., Garnett J.A., Zhou M., Li Y., Peng Z., Taylor J.D.,
RA Lee W.C., Bodey A., Murray J.W., Alguel Y., Bergeron J., Bardiaux B.,
RA Sawyer E., Isaacson R., Tagliaferri C., Cota E., Nilges M., Simpson P.,
RA Ruiz T., Wu H., Matthews S.;
RT "Structural insights into serine-rich fimbriae from gram-positive
RT bacteria.";
RL J. Biol. Chem. 285:32446-32457(2010).
CC -!- FUNCTION: The major structural element of fimbriae. Required for
CC adherence to saliva-coated hydroxyapatite beads (SHA), an in vitro
CC tooth model. A Fap1-dependent increase in adherence is seen as the pH
CC is reduced from pH 8 to pH 5. {ECO:0000269|PubMed:10594831,
CC ECO:0000269|PubMed:9632253}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Secreted, cell wall;
CC Peptidoglycan-anchor. Fimbrium. Note=Primarily but not exclusively
CC exported by the accessory SecA2/SecY2 protein translocation apparatus.
CC -!- INDUCTION: Low expression in early log phase, it increases until
CC stationary phase (at protein level). A monocistronic transcript.
CC {ECO:0000269|PubMed:10594831, ECO:0000269|PubMed:9632253}.
CC -!- DOMAIN: Has short and long regions consisting of (E/V/I)S dipeptide
CC repeats. These Ser-rich regions have 28 and 1000 repeats respectively.
CC {ECO:0000269|PubMed:10594831}.
CC -!- PTM: Glycosylated; occurs within the cytoplasm (PubMed:16997950,
CC PubMed:9632253, PubMed:20164186). It is probable that most of the Ser
CC residues in SSR1 and SSR2 are O-GlcNAcylated. Sequential glycosylation
CC by sugar transferases are able to generate complex sugar polymorphisms
CC (By similarity). {ECO:0000250|UniProtKB:A0A0H2URK1,
CC ECO:0000269|PubMed:16997950, ECO:0000269|PubMed:20164186,
CC ECO:0000269|PubMed:9632253}.
CC -!- DISRUPTION PHENOTYPE: Loss of fimbriae on the cell surface, loss of
CC adherence to saliva-coated hydroxyapatite beads (SAH), an in vitro
CC tooth model. {ECO:0000269|PubMed:10594831, ECO:0000269|PubMed:9632253}.
CC -!- SIMILARITY: Belongs to the serine-rich repeat protein (SRRP) family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-18 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79868.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AF100426; AAC79868.1; ALT_INIT; Genomic_DNA.
DR EMBL; DQ990875; ABL73998.1; -; Genomic_DNA.
DR PIR; T17451; T17451.
DR PDB; 2KUB; NMR; -; A=213-293.
DR PDB; 2X12; X-ray; 2.90 A; A/B=191-522.
DR PDB; 3RGU; X-ray; 3.00 A; A/B/C/D=201-316.
DR PDBsum; 2KUB; -.
DR PDBsum; 2X12; -.
DR PDBsum; 3RGU; -.
DR AlphaFoldDB; A1C3L3; -.
DR SMR; A1C3L3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR007383; DUF445.
DR InterPro; IPR022263; KxYKxGKxW.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR026465; Ser_adhes_glycop.
DR Pfam; PF04286; DUF445; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF19258; KxYKxGKxW_sig; 1.
DR TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
DR TIGRFAMs; TIGR04224; ser_adhes_Nterm; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell wall; Cytoplasm;
KW Direct protein sequencing; Fimbrium; Glycoprotein; Peptidoglycan-anchor;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..85
FT /evidence="ECO:0000269|PubMed:9632253"
FT CHAIN 86..2554
FT /note="Fap1 adhesin"
FT /id="PRO_0000414882"
FT PROPEP 2555..2587
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000414883"
FT REGION 107..195
FT /note="Ser-rich region 1, SRR1"
FT REGION 107..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..522
FT /note="Sufficient to block adherence to beads"
FT REGION 515..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..2561
FT /note="Ser-rich region 2, SRR2"
FT REGION 568..2558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2367..2587
FT /note="Required for localization to cell wall, fimbriae
FT formation and adherence to saliva-coated hydroxyapatite
FT beads (SHA) but not secretion"
FT MOTIF 2551..2555
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2554
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 219
FT /note="I->A: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 223
FT /note="E->A: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 227
FT /note="D->A: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 248
FT /note="L->A: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 249
FT /note="V->A: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 289
FT /note="E->A: Adheres to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 376..377
FT /note="IL->AA: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 385
FT /note="L->A: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 470
FT /note="L->A: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 488
FT /note="N->A: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 490
FT /note="Q->A: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT MUTAGEN 496
FT /note="I->A: Loss of adherence to SHA."
FT /evidence="ECO:0000269|PubMed:20584910"
FT CONFLICT 461
FT /note="K -> E (in Ref. 1; AAC79868)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="T -> A (in Ref. 1; AAC79868)"
FT /evidence="ECO:0000305"
FT CONFLICT 1146
FT /note="V -> P (in Ref. 1; AAC79868)"
FT /evidence="ECO:0000305"
FT CONFLICT 1226
FT /note="I -> S (in Ref. 1; AAC79868)"
FT /evidence="ECO:0000305"
FT CONFLICT 1830
FT /note="V -> M (in Ref. 1; AAC79868)"
FT /evidence="ECO:0000305"
FT CONFLICT 1861
FT /note="S -> P (in Ref. 1; AAC79868)"
FT /evidence="ECO:0000305"
FT CONFLICT 1885
FT /note="S -> T (in Ref. 1; AAC79868)"
FT /evidence="ECO:0000305"
FT HELIX 216..234
FT /evidence="ECO:0007829|PDB:3RGU"
FT HELIX 238..263
FT /evidence="ECO:0007829|PDB:3RGU"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:3RGU"
FT HELIX 269..293
FT /evidence="ECO:0007829|PDB:3RGU"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:2X12"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:2X12"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:2X12"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 364..371
FT /evidence="ECO:0007829|PDB:2X12"
FT TURN 373..377
FT /evidence="ECO:0007829|PDB:2X12"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 399..409
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 442..450
FT /evidence="ECO:0007829|PDB:2X12"
FT HELIX 454..459
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 461..471
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:2X12"
FT STRAND 498..510
FT /evidence="ECO:0007829|PDB:2X12"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:2X12"
SQ 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
