ID U2Y0S3_STRAP Unreviewed; 2184 AA.
AC U2Y0S3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Gram-positive cocci surface proteins LPxTG domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ANG6_0811 {ECO:0000313|EMBL:GAD46316.1};
OS Streptococcus anginosus T5.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1163302 {ECO:0000313|EMBL:GAD46316.1, ECO:0000313|Proteomes:UP000016981};
RN [1] {ECO:0000313|EMBL:GAD46316.1, ECO:0000313|Proteomes:UP000016981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T5 {ECO:0000313|EMBL:GAD46316.1,
RC ECO:0000313|Proteomes:UP000016981};
RA Maruyama F., Sakurai A., Ogura Y., Homma H., Takahashi N., Ohtsubo Y.,
RA Hoshino T., Okahashi N., Nakagawa I., Kimura S., Fujiwara T., Hayashi T.,
RA Shintani S.;
RT "Genome Sequences of seven clinical isolates and type strains of anginosus
RT group streptococci.";
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD46316.1}.
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DR EMBL; BASY01000006; GAD46316.1; -; Genomic_DNA.
DR RefSeq; WP_022526404.1; NZ_BASY01000006.1.
DR Proteomes; UP000016981; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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; -; 14.
DR Gene3D; 2.60.40.740; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR013783; Ig-like_fold.
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; 14.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF12892; FctA; 14.
DR Pfam; PF17802; SpaA; 1.
DR SUPFAM; SSF49401; Bacterial adhesins; 2.
DR SUPFAM; SSF49478; Cna protein B-type domain; 1.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW 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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..2184
FT /note="Gram-positive cocci surface proteins LPxTG domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039021613"
FT TRANSMEM 2160..2180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 167..264
FT /note="SDR-like Ig"
FT /evidence="ECO:0000259|Pfam:PF17961"
FT DOMAIN 452..513
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 540..648
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 658..762
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 770..886
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 894..1006
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 1015..1120
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 1129..1233
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 1242..1356
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 1365..1470
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 1479..1582
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 1592..1696
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 1705..1809
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 1817..1922
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 1931..2035
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT DOMAIN 2044..2148
FT /note="Streptococcal pilin isopeptide linker"
FT /evidence="ECO:0000259|Pfam:PF12892"
FT REGION 30..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2184 AA; 242391 MW; FF10854B4408BD91 CRC64;
MIKKAMNLVG VALLLASTIL SPASAVAQTL SNQSSTVTTQ SSSKTGTTEQ PTSPTESTQK
TADTSSSQGQ QPATENKAEA NSNEQENKPS TSKEESSDAS QVKEETSSQK ANKVEEKSET
QPGAPPAAKD AKDIQAAPKT QRAPKEIDAI TKFSITDHNG KPLDKPLQQW EQFKIDGQFK
LPNNDVHEGD YTTFKISENL VLVSTPNFDI KDKDGQVVAR ATIDPENRLL KLTYTKYVEN
KSDVSGSFYF YTYVNHHIVK EKKKVPLQIT VNRNIVPIGE VEFGGLTPPS QKDLTKVGNF
KPDNTITYDI TVNQSGKEVP DAKVTDILKT PNISYVKDSF EIYKGKWVIK DNRWVLENKK
TVTNQFNVEF LSDSEFSIKL GKINKDEGYH IKYKAKANYK LQSGEVVENV ASLWSSQTKI
IDSIAKTTYL EAGGSAEGYV YSITLHKKDE TSGASLAGAV FRVTRDRNGA VVGDFTTDST
GKVTIPNLLK DNYTIKEIKA PDGYQLTGKE IRVKPEDFGT TKSITKDIVN KKNEKVSAQL
QVQKELIGRK LQKNEFEFDL KENGQVLQTV KNAADGKVQF KELEYTKAGT YHYTISEKAG
DVPGVEYEPN LISATVTVED KGGKLEVTKV TYSKAGEETK NPTFENRYAP GKTFARLEVN
KVLTGRQLQK DEFEFELTGK EDHIHQTKKN TAAGKVQFDT VEYTKAGEYH YTIKEKNNGL
GGITYDPKEI KVTVKVTDDG KGKLNSEIFY ENDDQTFKNT YSATKTNVQL SVKKVLTGRK
LKAQEFEFDL VDNTEVSPTV GKILQTVKNN ANGEVNFKSL EYTKAGTYEY FIRENKGSAP
GVTYDQKFIT VTVEVKEKSG KLEVSKVTYM TDGEEIKKPT FNNRYTPVKT SAKLEVKKVL
TGRPLQEGEF EFELKDLQRN KKILETVKNT ADGKVQFKEL KYTKAGIYHY TISEKAGDVP
GVEYEPNLIS ATVTVEDKGG KLEVTKITYS KAGEETKNPT FENRYTPGKT FARLEVNKVL
TGRQLQKDEF EFELKEDGKP DVLQTAKNDA QGKVQFQVIN YDKAGEYHYT ITEKKGQLGG
ITYDPKEVKA TVKITDDGKG KLHSEIVYEK NDTTFNNTYT TQATSATFDV TKELTGRKLK
AQEFEFELKE DGKPDVLQTA KNDAKGKVQF QAINYDKAGE YHYTITEKNN GLTGVTYDSS
KVKVTVKVTD DGKGKLSASV TYDGGKKTFK NTFTPKEITV PLQVTKALTG RNLQDDEFEF
ELYDGQNKLL QTVKNKADGT IPFKALKFTK TGLYNYLIKE KAGKVPGVGY DKQPIKVTIR
VQQEEDGQLI YNIVYLGLDE SGKNKISKQS FTNKYTAKGT DATFSVTKKL AGRALKDGEF
SFELKEDGKA DVLQTKKNDK AGKVQFDAIK YQTVGTHKYT ITEKNTGLGG VTYDTKTIKV
TVEVTDNGKG QLVSKVTYEN NDQTFNNTYS SQKVSAQLGV TKELTGRALN DQEFEFELVG
SDDNVRQTKK NAADGRVTFD AIDYTKVGTY HYTIKEKDNG LGGVTYDKKE IKATVKVTDD
GNGQLVAQVS YDTANPTFSN TYLAKETTAT LEANKVLTGR DLEANEFAFD LIDPNGKVVD
TVKNAKDGKI SFKELTFKTA GTYTYTIKEQ AGALGGVKYD TKVIKATVTV TDDGKGQLHT
TVAYENNQNT FTNTYSADKA TATLSAKKLL EGRNLKEGEF EFELTGTDDQ VRQTKTNAQD
GSVTFDTIEY TKVGTYHYTI TEKDTKLGGV KYDTKVIKAT VTVTDDGQGH LVTKVAYEKD
DQTFKNTYSA AKTNAQLSVK KTLTGRALKD GEFEFELKGQ DDKVTQSKKN AQDGSVTFDT
IEYTKAGTYH YTITEKNTRL GGVTYDKKVI KATVTVTDNG QGQLVAQVAY EQNDQTFTNQ
YQAASTTAQL SANKQLTGRD LKAGEFSFEL KNDKDEVLET ATNDKDGKIT FKTLTYTAVG
TYQYTIIEKD TKLGGVKYDT KVIKATVTVT DNGAGKLVAT VSYDTKDRVF NNTYTADSVQ
ATVEVTKKLV GRTLKANEFE FVLKDERGQV LQTKKNTADG SVNFDAFEYK TTGTYHYTIA
EKDTKLQGIT YDKKVIKVTV TVTDDGNGHL VAKVSYDKNI KTFENRYTPP KKGLPKTGTV
IHTVAIFIGL IVLVGAVYLI KKKS
//
