ID Q9KK50_STREE Unreviewed; 655 AA.
AC Q9KK50;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 13-SEP-2023, entry version 75.
DE SubName: Full=Surface protein PspC {ECO:0000313|EMBL:AAF73777.1};
GN Name=pspC {ECO:0000313|EMBL:AAF73777.1};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:AAF73777.1};
RN [1] {ECO:0000313|EMBL:AAF73777.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=8R1 {ECO:0000313|EMBL:AAF73777.1};
RX PubMed=11891047; DOI=10.1016/S0378-1119(01)00896-4;
RA Iannelli F., Oggioni M.R., Pozzi G.;
RT "Allelic variation in the highly polymorphic locus pspC of Streptococcus
RT pneumoniae.";
RL Gene 284:63-71(2002).
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DR EMBL; AF154010; AAF73777.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KK50; -.
DR Gene3D; 1.20.81.20; -; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 2.
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; NF033838; PspC_subgroup_1; 1.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR Pfam; PF01473; Choline_bind_1; 2.
DR Pfam; PF19127; Choline_bind_3; 2.
DR Pfam; PF05062; RICH; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR PROSITE; PS51170; CW; 7.
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 53..135
FT /note="RICH"
FT /evidence="ECO:0000259|Pfam:PF05062"
FT REPEAT 476..495
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 496..515
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 516..535
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 536..555
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 556..575
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 576..595
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 596..615
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 73951 MW; 30623F1EDB9D05C2 CRC64;
MFASKSERKV HYSIRKFSIG VASVAVASLF LGGVVHAEGV GGRNTSTVTS SGQDTSKKYA
DEVKSHYQSI LEKVRKSLEK DRHTQNVGLI TKLSEIKKKY LYELEVNVLL EEKSKAELPS
KAKAELDAAF EQFKKEPELT KKVAEAQKKV EEAKKKAEDQ KEEDFRNYPT NTYKTIELEI
AESDVKVKEA ELELLKEEAK EHRDEGTIKQ VEEKVKSEKA EATRLEEIKT ERKKAEEEAK
RRADAKEQGK PKGRAKRGVP GEQATPDKKE NDAKSSDSSV GEETLPNPSL KPEKKVAEAQ
KKVEEAKKKA KDQKEEDHRN YPTITYKTLE LEIAESDVEV KKAELELVKE EAKGSRNEEK
VKQAKAEVES KKAEATRLEK IKTDRKKAEE AKRKAAEEDK VKEKPAEQPQ PAPAPQPEKP
APAPKPENPA EQPKAEKPAD QQAEEDYARR SEEEYNRLTQ QQPPKTEKPA QPSTPKTGWK
QENGMWYFYN TDGSMATGWL QNNGSWYYLN ANGSMATGWL QNNGSWYYLN ANGAMATGWL
QNNGSWYYLN ANGDMATGWL QNNGSWYYLN ANGSMVTGWL QNNGSWYYLN ANGSMATDWV
KDGDTWYYLE ASGAMKASQW FKVSDKWYYV NGSGALAVNT TVDSYRVNAN GEWVN
//