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Database: UniProt
Entry: F0FGP9_STRSA
LinkDB: F0FGP9_STRSA
Original site: F0FGP9_STRSA 
ID   F0FGP9_STRSA            Unreviewed;      1405 AA.
AC   F0FGP9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=LPXTG-motif cell wall anchor domain protein {ECO:0000313|EMBL:EGC21906.1};
DE            EC=3.2.1.80 {ECO:0000313|EMBL:EGC21906.1};
GN   ORFNames=HMPREF9388_1882 {ECO:0000313|EMBL:EGC21906.1};
OS   Streptococcus sanguinis SK353.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=888815 {ECO:0000313|EMBL:EGC21906.1, ECO:0000313|Proteomes:UP000004185};
RN   [1] {ECO:0000313|EMBL:EGC21906.1, ECO:0000313|Proteomes:UP000004185}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK353 {ECO:0000313|EMBL:EGC21906.1,
RC   ECO:0000313|Proteomes:UP000004185};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC       {ECO:0000256|ARBA:ARBA00009902}.
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:EGC21906.1}.
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DR   EMBL; AEWY01000011; EGC21906.1; -; Genomic_DNA.
DR   RefSeq; WP_002898976.1; NZ_GL872307.1.
DR   PATRIC; fig|888815.3.peg.1852; -.
DR   HOGENOM; CLU_005855_0_0_9; -.
DR   Proteomes; UP000004185; Unassembled WGS sequence.
DR   GO; GO:0051669; F:fructan beta-fructosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18622; GH32_Inu-like; 1.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 1.20.1270.90; AF1782-like; 1.
DR   Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR025883; Cadherin-like_b_sandwich.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011098; G5_dom.
DR   InterPro; IPR001362; Glyco_hydro_32.
DR   InterPro; IPR018053; Glyco_hydro_32_AS.
DR   InterPro; IPR013189; Glyco_hydro_32_C.
DR   InterPro; IPR013148; Glyco_hydro_32_N.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR022263; KxYKxGKxW.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   PANTHER; PTHR42800; EXOINULINASE INUD (AFU_ORTHOLOGUE AFUA_5G00480); 1.
DR   PANTHER; PTHR42800:SF1; EXOINULINASE INUD (AFU_ORTHOLOGUE AFUA_5G00480); 1.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF12733; Cadherin-like; 1.
DR   Pfam; PF07501; G5; 1.
DR   Pfam; PF08244; Glyco_hydro_32C; 1.
DR   Pfam; PF00251; Glyco_hydro_32N; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   SMART; SM00635; BID_2; 1.
DR   SMART; SM01208; G5; 1.
DR   SMART; SM00640; Glyco_32; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   PROSITE; PS51109; G5; 1.
DR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EGC21906.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGC21906.1};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1259..1334
FT                   /note="G5"
FT                   /evidence="ECO:0000259|PROSITE:PS51109"
FT   DOMAIN          1373..1405
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          85..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1204..1241
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        85..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1405 AA;  156304 MW;  1B14552D9830A1CA CRC64;
     MKNHQEKVCK NWFMRKSGKR WVFGCALLAF GAFLLDGGGV VYADEGKANP APAQVLQTDS
     SAVSEPESGQ TAALTMNADK VENSVAGETA TTEAGSQDAA VESANQKADK EDQVTANARE
     TKQEEDEQTA AKEVVSEKLP AAETVDKQSG FNTNLAEAKG DKNGVWEVRE QGLYSDARGK
     GDSFLYSQSQ GKDFVYSTDV TFLSKEGAAA LIFRGNNNPD DKSSYAVNID GGSNNVKFWR
     WQGGRDYQFI NEKHIEPTDD NKYRLKVVSI GSWVSYYVND ILVASSGDYT LQRDDKGQNT
     YLSEGYFGLL NWNSELLFQN TFYKEITPQS NPELEDIRVT SSVGKVEQKG QFTAPITIQY
     VKHDAETVDL TAVAKNPAAK VSVTDAAGRV YSDLKNVPLA VGANYLTVTS TVTDADGQEV
     SLTYRLNVHR RQADEIYYNE LYRGQYHYSV KDGWANDPNG LVYYKGVYHF FYQFYDDTKW
     GPMHWGHATS KDLIHWEEQP IAFYPDANGA MFSGSIVADT TNSSGLFDND QGGLIALITA
     DGNGQRIKLA YSKDEGRTWT KLDQIAADWT DDPLQSQDFR DPKVFRWEGK WFMVVAGGPL
     RIYSSDNLRN WKVESTYADL HTECPDLYPL LADDGSLKWV LSRGGRSYKV GDFRQVAGKW
     TFVPDAEFAQ ADQVMNFGKD SYAAMTYYVQ DFGSKANPTL PDIIESNWMN TWEDYCNLVA
     DTVGQKFNGT FNLNLKLGLI KQDRSYRLTQ TPITAYQSLR QEDKAVLYKD VEVSEKNELL
     KDFSGDQYEI VSTFRPSETT KKVGFNLRVG DGEVTRVTYD LEKEILSIDR SQSGILLSNK
     FAQVDSQSVK RNADGSIDLH LYVDRSSLEV FAKGYTVAGA NQIFPAPNSL AARVFVEGGA
     AKADIALYPL KGIWKDKQVV TKPLELVQAS PVTNNIYVGD TLDLKAYVMP ATVSQAVSWS
     VDQPDLVSVT EDGNKLRVTA LQRGVVKVTA TSKENPNLSK VFTINISRND FKTNVPDLKA
     VSGKWYVDGE SLYNQNTSAN DYYMGGQKIP FPEYNLDVDL KYQKGLINIF YASENVDPRN
     AYSIQFGDND KIRLYRFMGE TIAESSMNGK HLNDGQFHHV KLVKTKNGVS VSVDGVEYLN
     HQFDTVEPYY NDAYVGLGLW DGDLEARNFF VTNLHEPAVN KASLQKVVDS TASLDPSLYT
     DETVQAYQSA LARAQSLLAD EKAEQADLDR AEQDLKTALA ALAVKPSHQV TPEEGIKDLV
     EEKPFLEIVM EEIAYQTREQ ENPELERGQR RILVAGQKGQ KRVFVEVLNG QRTVLGQEVL
     SLAVDELVEV GSKVVAESAK QPLTRTQPHA LNQGKEEKVI LSPRLQPAPD SALPKTGTQE
     DKFLTLAGLA FLGMGLLAGR KKQED
//
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