CPA_STRPY
ID CPA_STRPY Reviewed; 680 AA.
AC S5FV19;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Pilus tip adhesin Cpa;
DE Flags: Precursor; Fragment;
GN Name=cpa;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS)
RP OF 8-222 IN COMPLEX WITH SPERMIDINE VIA A COVALENT LINKAGE, FUNCTION,
RP IDENTIFICATION BY MASS SPECTROMETRY, CROSS-LINKS, AND SUBUNIT.
RC STRAIN=90/306S / Serotype M5;
RX PubMed=24220033; DOI=10.1074/jbc.m113.523761;
RA Linke-Winnebeck C., Paterson N.G., Young P.G., Middleditch M.J.,
RA Greenwood D.R., Witte G., Baker E.N.;
RT "Structural model for covalent adhesion of the Streptococcus pyogenes pilus
RT through a thioester bond.";
RL J. Biol. Chem. 289:177-189(2014).
CC -!- FUNCTION: Component of the pilus tip. Can bind covalently, via its two
CC reactive thioester bonds, to molecular targets from host cell surface
CC and can thus mediate adhesion of the streptococcal pili to host cells.
CC Lysine side chains or a carbohydrate with a free amine group might be
CC candidates for Cpa binding. In vitro, can covalently bind to
CC spermidine, but it is unlikely that spermidine is the natural target of
CC Cpa. {ECO:0000269|PubMed:24220033}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24220033}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250}.
CC -!- PTM: Proteolytically processed and assembled in pili through a
CC transpeptidation reaction catalyzed by a sortase, which leads to a
CC covalent link between Cpa and a major pilin subunit. {ECO:0000305}.
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DR EMBL; KC622314; AGQ45688.1; -; Genomic_DNA.
DR PDB; 4C0Z; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=8-222.
DR PDBsum; 4C0Z; -.
DR AlphaFoldDB; S5FV19; -.
DR SMR; S5FV19; -.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR023849; CHP03934_TQXA.
DR InterPro; IPR046022; DUF5979.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041033; Prealbumin-like.
DR InterPro; IPR013552; Thioester_dom.
DR Pfam; PF19407; DUF5979; 1.
DR Pfam; PF17802; SpaA; 1.
DR Pfam; PF08341; TED; 2.
DR TIGRFAMs; TIGR03934; TQXA_dom; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Fimbrium; Isopeptide bond; Thioester bond.
FT CHAIN <1..675
FT /note="Pilus tip adhesin Cpa"
FT /id="PRO_0000425618"
FT PROPEP 676..>680
FT /note="Removed by sortase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000425619"
FT DOMAIN 253..311
FT /note="CNA-B"
FT REGION 217..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 672..676
FT /note="VPPTG sorting signal"
FT /evidence="ECO:0000255"
FT CROSSLNK 62..211
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT CROSSLNK 243..546
FT /note="Isoaspartyl lysine isopeptide (Lys-Asp)"
FT CROSSLNK 374..526
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000305"
FT CROSSLNK 562..667
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn)"
FT CROSSLNK 675
FT /note="Threonyl lysine isopeptide (Thr-Lys) (interchain
FT with K-? in major pilin subunit)"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 680
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:4C0Z"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4C0Z"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4C0Z"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:4C0Z"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4C0Z"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:4C0Z"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:4C0Z"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:4C0Z"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:4C0Z"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4C0Z"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:4C0Z"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:4C0Z"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:4C0Z"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4C0Z"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:4C0Z"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:4C0Z"
SQ SEQUENCE 680 AA; 76382 MW; B4B95297A33B1FBB CRC64;
GFSIRAFGAE EQSVPNKQSS VQDYPWYGYD SYSKGYPDYS PLKTYHNLKV NLDGSKEYQA
YCFNLTKHFP SKSDSVRSQW YKKLEGTNEN FIKLADKPRI EDGQLQQNIL RILYNGYPND
RNGIMKGIDP LNAILVTQNA IWYYTDSSYI SDTSKAFQQE ETDLKLDSQQ LQLMRNALKR
LINPKEVESL PNQVPANYQL SIFQSSDKTF QNLLSAEYVP DTPPKPGEEP PAKTEKTSVI
IRKYAEGDYS KLLEGATLKL AQIEGSGFQE KIFDSNKSGE KVELPNGTYV LSELKPPQGY
GVATPITFKV AAEKVLIKNK EGQFVENQNK EIAEPYSVTA FNDFEEIGYL SDFNNYGKFY
YAKNTNGTNQ VVYCFNADLH SPPDSYDHGA NIDPDVSESK EIKYTHVSGY DLYKYAVTPR
DKDADLFLKH IKKILDKGYK KKGDTYKTLT EAQFRAATQL AIYYYTDSAD LTTLKTYNDN
KGYHGFDKLD DATLAVVHEL ITYAEDVTLP MTQNLDFFVP NSSRYQALIG TQYHPNELID
VISMEDKQAP IIPITHKLTI SKTVTGTIAD KKKEFNFEIH LKSSDGQAIS GTYPTNSGEL
TVTDGKATFT LKDGESLIVE GLPSGYSYEI TETGASDYEV SVNGKNAPDG KATKASVKED
ETVAFENRKD LVPPTGLTTD
