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Database: UniProt
Entry: F2WWN4_STREE
LinkDB: F2WWN4_STREE
Original site: F2WWN4_STREE 
ID   F2WWN4_STREE            Unreviewed;       792 AA.
AC   F2WWN4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   13-SEP-2023, entry version 51.
DE   SubName: Full=Pneumococcal surface protein C {ECO:0000313|EMBL:ADZ45260.1};
GN   Name=pspC {ECO:0000313|EMBL:ADZ45260.1};
OS   Streptococcus pneumoniae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313 {ECO:0000313|EMBL:ADZ45260.1};
RN   [1] {ECO:0000313|EMBL:ADZ45260.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PMEN15 {ECO:0000313|EMBL:ADZ45260.1}, and PMEN16
RC   {ECO:0000313|EMBL:ADZ45261.1};
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:ADZ45260.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PMEN15 {ECO:0000313|EMBL:ADZ45260.1}, and PMEN16
RC   {ECO:0000313|EMBL:ADZ45261.1};
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; HQ264161; ADZ45260.1; -; Genomic_DNA.
DR   EMBL; HQ264162; ADZ45261.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2WWN4; -.
DR   SMR; F2WWN4; -.
DR   Gene3D; 1.20.81.20; -; 2.
DR   Gene3D; 1.20.58.440; choline binding protein A; 1.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR007756; RICH.
DR   InterPro; IPR038183; RICH_sf.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   NCBIfam; NF033839; PspC_subgroup_2; 2.
DR   NCBIfam; TIGR01168; YSIRK_signal; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF05062; RICH; 2.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   4: Predicted;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          761..792
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          274..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          122..223
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          560..591
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        275..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..525
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..646
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..727
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   792 AA;  88851 MW;  1E2089B2C0B97572 CRC64;
     MFASKSERKV HYSIRKFSIG VASVVVASLF LGGVVHAEEV RRGNNLTVTS SGDEVESHYQ
     SILEKVRKSL EKDRHTQNVD LIKKLQDIKR TYLYSLKEKP EAELTSKTKK ELDAAFEKFK
     KEPELTKKLA EAEKKVAEAE KKAKDQKEED HRNYPTNTYK TIELEIAEAE VGVAKAELEL
     ELAQAQVQIP QDTEKINAAK AKVEAAKSNV KKLEKIKSDI EKTYLYKLDN STKKTPKPRV
     RRNSPEIKAK GRVKNYKEAN IELSKYMTDL YKLDNSTKET PKSRVRRNSP QVGDSRELKE
     TIDKAKETLS TYMVTRLTKL DPSVFWFADL LMDAKKVVEE YKTKLEDASD KKSVEDLRKE
     AEGKIESLIV THQNREKENQ PAPQPGGQAG GSMVVPPVTQ TPPSTSQSPG QKATEAEKKK
     LQDLIRQFQE ALNKLDDETK TVPDGAKLTG EAGKAYNETR TYAKEVVDKS KKLLSQTAVT
     MDELAMQLTK LNDAMSKLKE AKAKLVPEVK PQPENPEPKP QPEGEKPSVP DINQEKEKAK
     LAIATYMSKI LDDIKKHHLK KEKHHQIVAL IKDLDKLKKQ ALSEIDNVNT KVEIENTVHK
     VFADMDAVVT KFKKGLTQDT PKEPGNKKPS APKPGMQPSP QPEVKPQLEK PKPEVKPQPE
     KPKPEVKPQL EKPKPEVKPQ PEKPKPEVKP QPEKPKPEVK PQPEKPKPEV KPQLEKPKPD
     NSKPQADDKK PSTTNNLSKD KQPSNQASTN EKATNKPKKS LPSTGSISNL ALEIAGLLTL
     AGATILAKKR MK
//
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