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Database: UniProt
Entry: U5P5V4_9STRE
LinkDB: U5P5V4_9STRE
Original site: U5P5V4_9STRE 
ID   U5P5V4_9STRE            Unreviewed;       690 AA.
AC   U5P5V4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Collagen-binding protein {ECO:0000313|EMBL:AGY38870.1};
GN   ORFNames=N597_07840 {ECO:0000313|EMBL:AGY38870.1};
OS   Streptococcus ilei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1156431 {ECO:0000313|EMBL:AGY38870.1, ECO:0000313|Proteomes:UP000017124};
RN   [1] {ECO:0000313|EMBL:AGY38870.1, ECO:0000313|Proteomes:UP000017124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I-P16 {ECO:0000313|Proteomes:UP000017124};
RA   Hyun D.-W.;
RT   "Genome sequence of Streptococcus SP. I-P16 isolated from human ileal
RT   fluid.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000256|ARBA:ARBA00004168}; Peptidoglycan-anchor
CC       {ECO:0000256|ARBA:ARBA00004168}.
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DR   EMBL; CP006776; AGY38870.1; -; Genomic_DNA.
DR   RefSeq; WP_023024420.1; NC_022582.1.
DR   AlphaFoldDB; U5P5V4; -.
DR   STRING; 1156433.N597_07840; -.
DR   KEGG; sip:N597_07840; -.
DR   PATRIC; fig|1156433.3.peg.1546; -.
DR   HOGENOM; CLU_002287_4_1_9; -.
DR   Proteomes; UP000017124; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   CDD; cd00222; CollagenBindB; 2.
DR   Gene3D; 2.60.40.1280; -; 1.
DR   Gene3D; 2.60.40.740; -; 1.
DR   Gene3D; 2.60.40.1140; Collagen-binding surface protein Cna, B-type domain; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   InterPro; IPR008454; Collagen-bd_Cna-like_B-typ_dom.
DR   InterPro; IPR008456; Collagen-bd_dom.
DR   InterPro; IPR011252; Fibrogen-bd_dom1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR041033; Prealbumin-like.
DR   InterPro; IPR041171; SDR_Ig.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   Pfam; PF17961; Big_8; 1.
DR   Pfam; PF05738; Cna_B; 2.
DR   Pfam; PF05737; Collagen_bind; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF17802; SpaA; 1.
DR   SUPFAM; SSF49401; Bacterial adhesins; 2.
DR   SUPFAM; SSF49478; Cna protein B-type domain; 3.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   4: Predicted;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Collagen {ECO:0000313|EMBL:AGY38870.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..690
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039492345"
FT   TRANSMEM        662..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          656..690
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          606..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..631
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  74638 MW;  19E58A9DCC416348 CRC64;
     MKKWLYAVVT TVALFLLAAL GFAKPNGVTK AHADTINDVV SSVNISKATG GDLTEPLGVW
     ESFNVEANFV LPNGRVKAGD QTVIQLGDGF KVFETDTIDL LDPTGQKVAT ATVDDQRKVI
     TVTYTDYPEK MANVTGKLRF FARVDHSVIK GNTTLDFTLS VDKTVISGGK VDYKGVNPGE
     YPPTPEVFSK WGWTNSGDKL KLTYTLNINQ GHTALHNIDI KDQLAFTDGK IKVDSVNIHT
     GTWKISDEDG AYHLGDTTNV TSHYSPVVSE DGRSLTVHIG DLAPEQGMTI RYDVYLDKVP
     AINTEYKNNA TMTATEVKEQ HKEADILYQF FEGAFNGEKY SFTIHKKGEN GQALAGAVFT
     VTADDTGEQV GTITTDEKGT GTVAGLIKQA YTVQEIQAPT GYVLSEEPIK ISKEDFGNDL
     AISREVINKK EKTSISGQKT WNDNDNHDGK RPSAITINLL ANGVKVASKE VKPDAEGNWL
     YQFDNLDVVD DTGNLIAYTV SEEPVAGYET SVEGTNITNS RTPEVTEVAV KKVWDDKENK
     DGLRPDKVTV RLLADGQEVA VKEITATDNW QASFTDLPVY KEGKKIVYTI TEDPVAGYTA
     TIDGFTVTNR HTPPTTPPPS TTTPPPASTT PSTTTPSTSE KPGTPTTPTE GKRKILPSTG
     EATSYGLFGA SALLALVGAA MLLSGKRKAD
//
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