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Database: UniProt
Entry: L7F7Y1_9ACTN
LinkDB: L7F7Y1_9ACTN
Original site: L7F7Y1_9ACTN 
ID   L7F7Y1_9ACTN            Unreviewed;      1035 AA.
AC   L7F7Y1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Tat pathway signal sequence domain protein {ECO:0000313|EMBL:ELP66795.1};
GN   ORFNames=STRTUCAR8_09521 {ECO:0000313|EMBL:ELP66795.1};
OS   Streptomyces turgidiscabies Car8.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP66795.1, ECO:0000313|Proteomes:UP000010931};
RN   [1] {ECO:0000313|EMBL:ELP66795.1, ECO:0000313|Proteomes:UP000010931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Car8 {ECO:0000313|EMBL:ELP66795.1,
RC   ECO:0000313|Proteomes:UP000010931};
RX   PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA   Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT   "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT   that shares virulence genes with other actinobacterial plant pathogens.";
RL   Plasmid 65:118-124(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:ELP66795.1}.
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DR   EMBL; AEJB01000327; ELP66795.1; -; Genomic_DNA.
DR   RefSeq; WP_006378056.1; NZ_AEJB01000327.1.
DR   AlphaFoldDB; L7F7Y1; -.
DR   STRING; 85558.T45_03803; -.
DR   PATRIC; fig|698760.3.peg.4424; -.
DR   Proteomes; UP000010931; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010931}.
FT   DOMAIN          46..202
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          206..314
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          321..474
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          646..742
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          755..856
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
FT   DOMAIN          890..1014
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|Pfam:PF00754"
FT   REGION          528..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1035 AA;  112164 MW;  58F8CF404DB4A797 CRC64;
     MTVTRRSVLV AGTSAPAAGA LLGTAADARA AAGRAGRRTV PLRDGWRFAL VDPGGLTDPT
     GAYADAPDPA YDDSTWRTVA VPHDWSIELA PTTDHGTTSG TGFFPGGLGW YRLAFTLPPA
     LAGKRISVEF DGVYMDSYVY CNGTELGRHP YGYTGFTIDL TDVLHTDGTT ENVLAVKVQN
     RLPSSRWYSG SGIYREARLV VTEPVHVERW GTYVTTPEIT EDRAVVQVRT SVLNASGAAA
     DVEVVSRIID PRGRTVARTS STVTVTDRSS ETHELTVPEP KLWDVAAPHR YTLKTDLRVG
     GATVDTHRTT FGIRSFRFDP DEGFQLNGTH HKIKGVDLHH DLGALGAAVS IDAIRRQMTV
     MKSMGVNAFR TSHNPPSPEM IQVCEELGIV MMVEAFDCWR SPKTRYDYGR FFDEWADKDI
     TEMVRAARNS PAVIMWSIGN EISEFTSTAG LTIADRLIAA VKASDDTRPI VIGSHRHRSV
     PAPGTPGDLI LAKLDGLGLN YNTAASVDAL HARYPHLFLF ESESSSETST RGAYQEPERL
     NTGENHTPGR RAVSSYDNNL ASWTMSGEYG LKKDRDRKWF AGEFLWSGID YIGEPTPYDV
     FPVKASFFGA VDTAGFPKDM YHLFRSQWTS EPMVHLLPMT WNHEPGDTVE VWAYANVDTV
     ELFLNGKSHG TRRFDTKKTA DGRPYLETTE ATGDDKTVTA GAWPGSYTSP TGSAGKLHLT
     WHVPYEPGEL KAVARRGGRV VATDVLRTAG PAHAIRLTAD RKSLAADGRS LCFVTADVVD
     ARGVVVPGAE HLLAFEVDGG SLAGLDNGRE ESAERYQAST RTAFHGKALA MVRAGTAAGR
     LKITARAAGL RTGTLTVRTT PAHDEALTPA TLFAPDPGPA APTYPLADAS YSGRPDSLPA
     AMLDGAPSTG WSNAFYKAPT ALLPAFSGAR AEDWISVDWG RARDFTRVEV SFTVDATHAL
     PASVAVSVWD GDRFVPVPDA SVHWSDTSDT PSAITFAAVR GARLRLDLTS RYPGEERGAV
     RISRVEAYWR SPSGV
//
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