PILIN_STRP1
ID PILIN_STRP1 Reviewed; 340 AA.
AC Q9A1S2; Q491J0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Pilin;
DE AltName: Full=Lancefield T antigen;
DE AltName: Full=Pilus backbone structural protein;
DE Flags: Precursor;
GN OrderedLocusNames=SPy_0128, M5005_Spy0109;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [3]
RP FUNCTION.
RX PubMed=17501921; DOI=10.1111/j.1365-2958.2007.05704.x;
RA Manetti A.G., Zingaretti C., Falugi F., Capo S., Bombaci M., Bagnoli F.,
RA Gambellini G., Bensi G., Mora M., Edwards A.M., Musser J.M., Graviss E.A.,
RA Telford J.L., Grandi G., Margarit I.;
RT "Streptococcus pyogenes pili promote pharyngeal cell adhesion and biofilm
RT formation.";
RL Mol. Microbiol. 64:968-983(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS), SUBUNIT, CROSS-LINKS, AND
RP MUTAGENESIS OF GLU-117 AND GLU-258.
RX PubMed=18063798; DOI=10.1126/science.1145806;
RA Kang H.J., Coulibaly F., Clow F., Proft T., Baker E.N.;
RT "Stabilizing isopeptide bonds revealed in Gram-positive bacterial pilus
RT structure.";
RL Science 318:1625-1628(2007).
CC -!- FUNCTION: Major component of the pilus. A stack of the pilin subunits,
CC joined by intermolecular isopeptide bonds, forms the pilus. The pilus
CC is required for bacterial adhesion to host cells, for bacterial
CC aggregation, and for biofilm formation. {ECO:0000269|PubMed:17501921}.
CC -!- SUBUNIT: Forms columns of about 3-nanometers in diameter of head-to-
CC tail-assembled molecules. {ECO:0000269|PubMed:18063798}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor.
CC Fimbrium. Note=Attached to the cell wall by a peptidoglycan anchor.
CC -!- PTM: Proteolytically processed and assembled in pili through a
CC transpeptidation reaction catalyzed by the sortase C1. The last pilin
CC subunit is cross-linked to the peptidoglycan.
CC -!- SIMILARITY: Belongs to the Streptococcus pilin family. {ECO:0000305}.
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DR EMBL; AE004092; AAK33238.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ50728.1; -; Genomic_DNA.
DR RefSeq; NP_268517.1; NC_002737.2.
DR PDB; 3B2M; X-ray; 2.22 A; A/B/C=18-305.
DR PDB; 3GLD; X-ray; 2.03 A; A/B/C=18-308.
DR PDB; 3GLE; X-ray; 2.19 A; A/B/C=18-308.
DR PDBsum; 3B2M; -.
DR PDBsum; 3GLD; -.
DR PDBsum; 3GLE; -.
DR AlphaFoldDB; Q9A1S2; -.
DR SMR; Q9A1S2; -.
DR PaxDb; Q9A1S2; -.
DR EnsemblBacteria; AAK33238; AAK33238; SPy_0128.
DR KEGG; spy:SPy_0128; -.
DR KEGG; spz:M5005_Spy0109; -.
DR PATRIC; fig|160490.10.peg.110; -.
DR HOGENOM; CLU_787371_0_0_9; -.
DR OMA; WTVDVYV; -.
DR EvolutionaryTrace; Q9A1S2; -.
DR Proteomes; UP000000750; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.3050; -; 1.
DR InterPro; IPR046022; DUF5979.
DR InterPro; IPR017503; Sortase_SrtB_sig_QVPTGV.
DR InterPro; IPR022464; Strep_pil_isopept_link.
DR InterPro; IPR038174; Strep_pil_link_sf.
DR Pfam; PF19407; DUF5979; 1.
DR Pfam; PF12892; FctA; 1.
DR TIGRFAMs; TIGR03065; srtB_sig_QVPTGV; 1.
DR TIGRFAMs; TIGR03786; strep_pil_rpt; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Fimbrium; Isopeptide bond; Peptidoglycan-anchor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..311
FT /note="Pilin"
FT /id="PRO_0000331363"
FT PROPEP 312..340
FT /note="Removed by sortase C1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000331364"
FT MOTIF 308..312
FT /note="EVPTG sorting signal"
FT /evidence="ECO:0000255"
FT SITE 117
FT /note="Autocatalyzes isopeptide 36-168 formation"
FT SITE 258
FT /note="Autocatalyzes isopeptide 179-303 formation"
FT MOD_RES 311
FT /note="Pentaglycyl murein peptidoglycan amidated threonine;
FT alternate"
FT /evidence="ECO:0000305"
FT CROSSLNK 36..168
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT CROSSLNK 161
FT /note="Threonyl lysine isopeptide (Lys-Thr) (interchain
FT with T-311)"
FT CROSSLNK 179..303
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT CROSSLNK 311
FT /note="Threonyl lysine isopeptide (Thr-Lys) (interchain
FT with K-161); alternate"
FT MUTAGEN 117
FT /note="E->A: Increased susceptibility to proteolysis."
FT /evidence="ECO:0000269|PubMed:18063798"
FT MUTAGEN 258
FT /note="E->A: Increased susceptibility to proteolysis."
FT /evidence="ECO:0000269|PubMed:18063798"
FT STRAND 31..42
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3GLD"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:3GLD"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 147..157
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 172..183
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:3GLE"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:3GLD"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:3GLD"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:3GLD"
SQ SEQUENCE 340 AA; 37188 MW; 9EB0C99CBF42161B CRC64;
MKLRHLLLTG AALTSFAATT VHGETVVNGA KLTVTKNLDL VNSNALIPNT DFTFKIEPDT
TVNEDGNKFK GVALNTPMTK VTYTNSDKGG SNTKTAEFDF SEVTFEKPGV YYYKVTEEKI
DKVPGVSYDT TSYTVQVHVL WNEEQQKPVA TYIVGYKEGS KVPIQFKNSL DSTTLTVKKK
VSGTGGDRSK DFNFGLTLKA NQYYKASEKV MIEKTTKGGQ APVQTEASID QLYHFTLKDG
ESIKVTNLPV GVDYVVTEDD YKSEKYTTNV EVSPQDGAVK NIAGNSTEQE TSTDKDMTIT
FTNKKDFEVP TGVAMTVAPY IALGIVAVGG ALYFVKKKNA
