ID D2JYC8_STREE Unreviewed; 908 AA.
AC D2JYC8;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 13-SEP-2023, entry version 48.
DE SubName: Full=PspC {ECO:0000313|EMBL:ACZ65025.1};
GN Name=pspC {ECO:0000313|EMBL:ACZ65025.1};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:ACZ65025.1};
RN [1] {ECO:0000313|EMBL:ACZ65025.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HU414/07 {ECO:0000313|EMBL:ACZ65025.1};
RX PubMed=22336290; DOI=10.1128/CVI.05706-11;
RA Moreno A.T., Oliveira M.L., Ho P.L., Vadesilho C.F., Palma G.M.,
RA Ferreira J.M.Jr., Ferreira D.M., Santos S.R., Martinez M.B., Miyaji E.N.;
RT "Cross-reactivity of antipneumococcal surface protein C (PspC) antibodies
RT with different strains and evaluation of inhibition of human complement
RT factor H and secretory IgA binding via PspC.";
RL Clin. Vaccine Immunol. 19:499-507(2012).
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DR EMBL; GU138640; ACZ65025.1; -; Genomic_DNA.
DR AlphaFoldDB; D2JYC8; -.
DR SMR; D2JYC8; -.
DR Gene3D; 1.20.81.20; -; 2.
DR Gene3D; 6.10.140.920; -; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 3.
DR Gene3D; 1.20.58.440; choline binding protein A; 2.
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; TIGR01168; YSIRK_signal; 1.
DR PANTHER; PTHR48148; KERATINOCYTE PROLINE-RICH PROTEIN; 1.
DR PANTHER; PTHR48148:SF2; KERATINOCYTE PROLINE-RICH PROTEIN; 1.
DR Pfam; PF01473; Choline_bind_1; 4.
DR Pfam; PF19127; Choline_bind_3; 2.
DR Pfam; PF05062; RICH; 2.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 2.
DR SUPFAM; SSF161270; PspA lactotransferrin-binding region; 1.
DR PROSITE; PS51170; CW; 9.
PE 4: Predicted;
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 69..146
FT /note="RICH"
FT /evidence="ECO:0000259|Pfam:PF05062"
FT DOMAIN 312..389
FT /note="RICH"
FT /evidence="ECO:0000259|Pfam:PF05062"
FT REPEAT 689..708
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 709..728
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 729..748
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 749..768
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 769..788
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 789..808
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 809..828
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 829..848
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 849..868
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 201..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 103322 MW; FD98379C5CFF9170 CRC64;
MFTSKSERKV HYSIRKFSIG VASVVVASLV MGSVVHATEN EGITQVATSY NKANESQTEH
RKAAKQVDED IKKMLSEIQE YIKKMLSEIQ LDKRKHTQNV NLNRKLSAIQ TKYLYELRVL
KEKSKKEELT SKTKKELDAA FEKFKKEPEL TKKLAEAKQK AKAQKEEDFR NYPTNTYKTL
ELEIAEFDVK VKEAELELVK EEAKPRNEEK IKQAKAKVES KKAEATRLEE IKTERKKAEE
EAKRKAEESE KKAAEAKQKV DTKEQGKPKR RAKRGVSGEL ATPDKKENDA KSSDSSVGEE
TLPSPSLNMA NESQTEHRKD VDEYIKKMLG EIQLDRRKHT QNVNLNIKLS AIKTKYLYEL
SVLKENSKKE ELTSKTKAEL TAAFEQFKKD TLKPEKKVAE AEKKVEEAKK KAKDQKEEDR
RNYPTNTYKT LELEIAESDV RVKEAELELV KEEASESRNE EKIKQAKEKV ESKKAEATRL
EKIKTDRKKA EEEAKRKAEE SEKKAAEAKQ KVDAEEYALE AKIAELEYEV QRPEKELKEI
DESDSEDYLK EGLRAPLQSK LDTKKAKLSK LEELSDKIDE LDAEIAKLEV QLKDAEGNNN
VEAYFKEGLE KTTAEKKAEL EKAEADLKKA VDEPETPAPA PQPAPAPEKP AEKPAPAPEK
PAPAPEKPAE KPAPAPAPEK PAPTPETPKT GWKQENGMWY FYNTDGSMAT GWLQNNGSWY
YLNSNGAMAT GWLQNNGSWY YLNSNGAMAT GWLQYNGSWY YLNANGDMAT GWFQYNGSWY
YLNANGDMAT GWFQYNGSWY YLNANGDMAT GWLQYNGSWY YLNSNGAMVT GWLQNNGSWY
YLNANGSMAT DWVKDGDTWY YLEASGAMKA SQWFKVSDKW YYVNGSGALA VNTTVDSYRV
NANGEWVN
//
