ID T0TQX5_9STRE Unreviewed; 1208 AA.
AC T0TQX5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Glycosyl hydrolase family29(Alpha-L-fucosidase) {ECO:0000313|EMBL:EQC75820.1};
GN ORFNames=HSISM1_70 {ECO:0000313|EMBL:EQC75820.1};
OS Streptococcus sp. HSISM1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1316408 {ECO:0000313|EMBL:EQC75820.1};
RN [1] {ECO:0000313|EMBL:EQC75820.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSISM1 {ECO:0000313|EMBL:EQC75820.1};
RA Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA Kleerebezem M.;
RT "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL PLoS ONE 8:E83418-E83418(2013).
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:EQC75820.1}.
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DR EMBL; ASKI01000088; EQC75820.1; -; Genomic_DNA.
DR AlphaFoldDB; T0TQX5; -.
DR PATRIC; fig|1316408.3.peg.1919; -.
DR eggNOG; COG3583; Bacteria.
DR eggNOG; COG3664; Bacteria.
DR eggNOG; COG3669; Bacteria.
DR HOGENOM; CLU_001189_1_0_9; -.
DR Proteomes; UP000015933; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR011098; G5_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR019931; LPXTG_anchor.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR PANTHER; PTHR10030:SF37; ALPHA-L-FUCOSIDASE; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07501; G5; 1.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SMART; SM00237; Calx_beta; 1.
DR SMART; SM01208; G5; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF141072; CalX-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51109; G5; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EQC75820.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1185..1204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 396..529
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1020..1099
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
FT DOMAIN 1175..1208
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 134535 MW; D3B187C6B360BFDD CRC64;
MFLGTTTSYA EEQAERSETR EERVETSNAG DQGKEEKTVN EHQEQSEQPS AATSEKENRT
VSQGTEASQP ATSLNEETEI ADYGPLPSKA QMQYHREELA AFIHFGMNTY YDREWGDGQE
DPYYFYPEHL DTDQWIKTLK DAGFKRTIMV VKHHDGFLLY PSKYTDHTIA KSGWKDGKGD
VLAEVSASAS KYDMDMGVYL SPWDAHSPLY HVDTEDQYNE YYLNQLKEIL EDPKYGNKGK
FVEVWMDGAR GDGAQKVTYT FDKWFEAIRK AQGDIAIFSA EPTNVRWIGN EKGIAGDPVW
QKVNPDKIRN NPSNSYLNHG DPEGKQYSVG EADVSIRSGW FYHDNQEPKS LRELMDIYFK
SVGRGTPLLL NIPPNQDGKF AEDDVARLKE FRQTLDQLYS VNYAAGALVE ADSTRRNSLY
KASHLTDGDE KTSWAPADDA KTGSFVLDLG KEQHFDVVEL KETIEKGQRI SGFTIDVAVN
GQWVPYGAGS TVGYRRLIKG QPVDSRYIRV SITDAQATPI LNGVSVYKTP ASIEETDGYP
LGLTYHSDRT ADRANGQWNE EGEGVRGTSM WTKEKGASVT YQFEGTKAYV VATVDPGYGE
MDVYVDGQKL ATVNTQSPSR KRSQKVYETP DLAAGSHTLT LVNSKGDAIA TEGIYALNNQ
EKGLFEFAQP TLAVKKGDLA QVVVKRKGGS KGSASLKLIT EPGTGVHGKV YKDTNVTLEF
ADGETEKTVQ VPTLDFAGKA TDVYDFKVKL LHPDQGSLVG FIPELTVQVM NEDQLPENRK
EVDDQDPKLH YSQGWHHETD NKDFSNGTES WSSFNQVTDE EGKKHIEVTI TFKGTGVEVR
GVVDPSHGLY SVTLDGKEIA FEEGRGHDYE IDGDHYFSGY GDQRKLDQSL VNLQGLAKGY
HQLRLHLDPA LNDPQSSRAI QVDQFILSGK DSQLLSQEEL QQIIREGVEK IKATSLDRLK
ADLKPTVQGQ LTDLTQLLDQ ERPDLVAAAN QIEALETILE AAHNYEPLTQ TRPEEGIRDL
ILEKPELLIE AEEIPFESQT RENKDLAKGE SRILQAGKVG RRLKLIEVRQ EEGKEIRTEV
DAFVEVEAQD QITEVGTKEA EKSPLIADMP TPTTPVTPSK VQPEVMTLSQ AEDKKEKGRP
VLLQPKTPEA VSVLTSDHPE KEVVESPSLQ SEGKLPQTGT KEGGFFAWLG LLGLGFLGGG
AKFARRKE
//
