ID   U5P5C7_9STRE            Unreviewed;      1408 AA.
AC   U5P5C7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Gram-positive cocci surface proteins LPxTG domain-containing protein {ECO:0000259|PROSITE:PS50847};
GN   ORFNames=N597_08365 {ECO:0000313|EMBL:AGY38969.1};
OS   Streptococcus ilei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1156431 {ECO:0000313|EMBL:AGY38969.1, ECO:0000313|Proteomes:UP000017124};
RN   [1] {ECO:0000313|EMBL:AGY38969.1, 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}.
CC   -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC       (SDr) family. {ECO:0000256|ARBA:ARBA00007257}.
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DR   EMBL; CP006776; AGY38969.1; -; Genomic_DNA.
DR   STRING; 1156433.N597_08365; -.
DR   KEGG; sip:N597_08365; -.
DR   PATRIC; fig|1156433.3.peg.1657; -.
DR   HOGENOM; CLU_002287_3_1_9; -.
DR   Proteomes; UP000017124; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 2.60.40.1280; -; 1.
DR   Gene3D; 2.60.40.3050; -; 5.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   InterPro; IPR008966; Adhesion_dom_sf.
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   InterPro; IPR022464; Strep_pil_isopept_link.
DR   InterPro; IPR038174; Strep_pil_link_sf.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   NCBIfam; TIGR03786; strep_pil_rpt; 5.
DR   PANTHER; PTHR36108:SF13; COLOSSIN-B; 1.
DR   PANTHER; PTHR36108; COLOSSIN-B-RELATED; 1.
DR   Pfam; PF17961; Big_8; 1.
DR   Pfam; PF12892; FctA; 5.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF17802; SpaA; 4.
DR   SUPFAM; SSF49401; Bacterial adhesins; 2.
DR   SUPFAM; SSF49478; Cna protein B-type domain; 2.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1408
FT                   /note="Gram-positive cocci surface proteins LPxTG domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004663086"
FT   DOMAIN          1376..1408
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          1333..1384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1338..1353
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1362..1378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1408 AA;  150721 MW;  9E1B503848478417 CRC64;
     MKKSLKIILT LVLVLASVFG LSKIRSAHAD GATGKIQITS KTITPTKSPV DQYTDIKVDL
     TFNVPNGVKP GDQAVITLPP NLKFIKDAEF EVRSPNGELV SEAVINAANK TITLTYQDYV
     KGKSNISGSM FFAVRVEPAT ASPSKVPITL NVDNNPVPVG EVDFVVDPGN AEKVLDKVSW
     DTKHLADGGI TRQYEVRVNA TKEPLTEAVV TDQLQTEGMS YVEDSFVIKK GNWAVNSSHK
     LDLKNGQVVS LPVEFGADKK SFKVSLGNVA QGEGYSIVYK VKIPYTPAND EKFFNNVTLN
     AKKVVETKSN PFVYQTEGGK AQGYTFSINL KKVDGQDENT ALAGAEFNVI RVATGAVVGK
     LTTNAKGEAS IGGLLNTAYQ LVETKAPEGY ELDATPIDVK SEDFGTTKTA LKTVTNKKIV
     KEPTPTSAVI ELDKALTGRD LVDGEFSFEL YEGANKLQTV TNKSGKVTFE SISYTAEGEH
     TYTVKEVKGD NATIAYDASE KQVTVKVTRD GDALKAEVVY PESKTFTNAF TPNATTATIE
     LTKELTGRDL VDGEFSFELY EGANKLQTVT NKSGKVTFES ISYTAEGEHT YTVKEVKGND
     ATITYDASEK QVTVKVTRDG DALKAEVVYP ESKTFTNSFT PKATTATIEL SKELTGRDLV
     DGEFSFELYE GANKLQTVTN KSGKVTFDAI SYTAEGEHTY TVKEVKGDNA TIAYDTAEKQ
     VTVKVTRDGD ALQAEVVYPE NKTFTNAFTP NATTATIELT KELTGRELVD GEFSFELYEG
     ANKLQTVTNK SGKVTFDAIS YTAEGEHTYT VKEVKGNVPG ITYDTAEKQV TVQVTKDGDN
     LKATVVYPES KVFANTYSAP SPAKAQISAS KILEGRDLKD GEFSFNLLDE AGEVLQTKQN
     AADGSVAFDE ISYSQEDAGK TFHYTIKEVI PQSQEKGMTY DQASIEVTVT VTKDDASNTI
     KATVAYGAKT SFTNTFVTSE IPPTPPVVEK PEAKLYTIQL HKVNGEGRAL AGAVFGLFEA
     DGSTPVANPY GEGQATATSD ANGLVSFVGF EAKDYVVKEL TAPEGYQLST ASIAVSATEL
     SAASDLVVDK GNVVNQPFTE IPPTPPVVEK PELTLYSIQL HKVNNEGKAL AGAVFGLFEA
     DGVTPVANPY GEGQATATSD ANGLVTFTGL EAKDYVVKEI TAPEGYQLSE EAITVSSNQL
     IASTNQVLDQ GKVVNKPFTA IPPTPPVVEK PELKLYTIQL HKVNGEGRAL AGAVFGLFEA
     DGSTPVANPY GEGQATATSD ANGLVSFVGF EAKDYVVKEL TAPAGYQLST NPITVTAEDY
     VQATDLVVDK GNVVNELTPP TPPTPPTTPP TTPSTDKPKG DKPSGSQPKE EKEHTLPSTG
     ETVSEGLVAT GLALAVAGSA LVYKKREN
//