ID F2WWM0_STREE Unreviewed; 917 AA.
AC F2WWM0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Pneumococcal surface protein C {ECO:0000313|EMBL:ADZ45246.1};
GN Name=pspC {ECO:0000313|EMBL:ADZ45246.1};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:ADZ45246.1};
RN [1] {ECO:0000313|EMBL:ADZ45246.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BHN78 {ECO:0000313|EMBL:ADZ45246.1};
RX PubMed=19494311; DOI=10.4049/jimmunol.0802376;
RA Dieudonne-Vatran A., Krentz S., Blom A.M., Meri S., Henriques-Normark B.,
RA Riesbeck K., Albiger B.;
RT "Clinical isolates of Streptococcus pneumoniae bind the complement
RT inhibitor C4b-binding protein in a PspC allele-dependent fashion.";
RL J. Immunol. 182:7865-7877(2009).
RN [2] {ECO:0000313|EMBL:ADZ45246.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BHN78 {ECO:0000313|EMBL:ADZ45246.1};
RA Hermans P.W.M., Albiger B.;
RT "Does binding to the complement inhibitor C4b-binding protein, facilitate
RT establishment and spread of multidrug-resistant pneumococcal clones in the
RT community?";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HQ264146; ADZ45246.1; -; Genomic_DNA.
DR AlphaFoldDB; F2WWM0; -.
DR Gene3D; 1.20.81.20; -; 2.
DR Gene3D; 2.10.270.20; -; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 2.
DR Gene3D; 1.20.58.440; choline binding protein A; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR007756; RICH.
DR InterPro; IPR038183; RICH_sf.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; NF033838; PspC_subgroup_1; 1.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR PANTHER; PTHR48125; LP07818P1; 1.
DR PANTHER; PTHR48125:SF10; RNA POLYMERASE II-ASSOCIATED FACTOR 1 HOMOLOG; 1.
DR Pfam; PF01473; Choline_bind_1; 1.
DR Pfam; PF19127; Choline_bind_3; 3.
DR Pfam; PF05062; RICH; 2.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 2.
DR PROSITE; PS51170; CW; 8.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 7..32
FT /note="YSIRK Gram-positive signal peptide"
FT /evidence="ECO:0000259|Pfam:PF04650"
FT DOMAIN 47..121
FT /note="RICH"
FT /evidence="ECO:0000259|Pfam:PF05062"
FT DOMAIN 479..560
FT /note="RICH"
FT /evidence="ECO:0000259|Pfam:PF05062"
FT REPEAT 718..737
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 738..757
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 758..777
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 778..797
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 798..817
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 818..837
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 838..857
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 858..877
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 317..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..214
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 506..537
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 340..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 102448 MW; AFF758460E15AA02 CRC64;
MFASKSERKV HYSIRKFSIG VASVVVASLF LGGVVHAEEV RRGNNLTVTS SGDEVESHYQ
SILEKVRKSL EKDRHTQNVD LIKKLQDIKR TYLYNLKEKP EAELTSKTKK ELDAAFEKFK
KEPELTKKLA EAEKKAKDQK EEDHRNYPTN TYKTIELEIA EAEVGVAKAE LELAQAQVQI
PQDTEKINAA KAKVEAAKSN VKKLEKIKSD IEKTYLYKLD NSTKETPKSR VRRNSPQVGD
SRELKETIDK AKETLSTYMV TRLTKLDPSV FWFADLLMDA KKVVEEYKTK LEDASDKKSV
EDLRKEAEGK IESLIVTHQN REKENQPAPQ PGGQAGGSMV VPPVTQTPPS TSQSPGQKAT
EAEKKKLQDL IRQFQEALNK LDDETKTVPD GAKLTGEAGK AYNETRTYAK EVVDKSKKLL
SQTAVTMDEL AMQLTKLNDA MSKLKEAKAK LVPEVKPQPE NPEPKPQPEG EKPSVPDINQ
EKEKAKLAIA TYMSKILDDI KKHHLKKEKH HQIVALIKDL DKLKKQALSE IDNVNTKVEI
ENTVHKVFAD MDTVVTKFQK GLIQNTPQVP EAPKSPEVPK VSDTPKAPDT PQVPEAPKSP
EVPKVPEAPK APDTPQVPEA PKSPEVPKVS DTPKAPDTPQ VPEAPKSPEV PKVPEAPKAP
DTPQVPEAPK SPEVPKVPDT PKAPDTPQVP EAPKAPDTPQ IPEAPAPETP APAPEAPKTG
WKQENGMWYF YNTDGSMATG WLEYNGSWYY LNANGAMATG WLEYNGSWYY LNTNGAMETG
WLEYNGSWYY LNTNGAMETG WLEYNGSWYY LNTNGAMETG WLEYNGSWYY LNTNGAMETG
WLEYNGSWYY LNANGSMATG WLKDGDTWYY LEASGAMKES QWFKVSDKWY YVNGSGALAV
NTTVGGYRVN ANGKWVN
//