ID   A0A089XDV6_STRGA        Unreviewed;      1095 AA.
AC   A0A089XDV6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Putative glycosyl hydrolase, family 2 {ECO:0000313|EMBL:AIS02193.1};
GN   ORFNames=SGLAU_31295 {ECO:0000313|EMBL:AIS02193.1};
OS   Streptomyces glaucescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1907 {ECO:0000313|EMBL:AIS02193.1, ECO:0000313|Proteomes:UP000029482};
RN   [1] {ECO:0000313|Proteomes:UP000029482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX   PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA   Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA   Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT   GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT   plasmid.";
RL   J. Biotechnol. 194:81-83(2015).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; CP009438; AIS02193.1; -; Genomic_DNA.
DR   RefSeq; WP_043505868.1; NZ_CP009438.1.
DR   AlphaFoldDB; A0A089XDV6; -.
DR   STRING; 1907.SGLAU_31295; -.
DR   KEGG; sgu:SGLAU_31295; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_009935_0_0_11; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000029482; Chromosome.
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; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR006558; LamG-like.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 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   Pfam; PF13385; Laminin_G_3; 1.
DR   Pfam; PF07691; PA14; 1.
DR   SMART; SM00560; LamGL; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51820; PA14; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AIS02193.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029482};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1095
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039583057"
FT   DOMAIN          55..199
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
FT   REGION          313..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1095 AA;  118984 MW;  F1212301EE1C855E CRC64;
     MTTRHTRRRT TLWALLTAAA LVLPTPGLTA TASATASAAE TSGGAPGLPV REAAAAVHGL
     KGEYFRMSAP GARDFAESGG TLLDPQINFS DLTGTFQELT GRTEHTTARW TGRIEPPVTG
     DYTFHAIGDN GFRLYIDGEP VIDHWVGDWD REQTSAPVTL TAGERHDFRL EMFQDTGGAG
     MFLRWSAPGL PKQLVPQSAF TPPDGFEVYP VEPSVSGNGR QVRARFEGDL GGDTGTVAGH
     LKIEADTTAM PIAGAAVAPG DPRSLLVTLA APIQKGQQVR LTYDGTGGLT SGGETVPRII
     RWARNDSTHR LTTPWGDKLD ERNPLPEYPR PQQVRSRWKN LNGPWQFSGA APGERPVFGK
     DLDERIIVPF PVESQLSGIE RHEDHMFYRR LVDVPKSWNV GTGGDGNRLV LNFGAVDHRA
     RVWVNGRQVT EHTGGYTAFS ADVTDALERT GPQEIVVAVT DTGGADQPKG KQSTHPGGIF
     YTQSSGIWQT VWMEPVARTS IDDIVTTPDI DSARLALTVE SDDASPAARV EAVARDARGR
     VVGRTSGPAN RELRLPVADQ HLWSPDDPYL YDLDVRLIDG RSTDRAGSYF GMREIGVEKV
     GGFRKLVLNG EPVFSLATLD QGFWPDGLYT PPSDAALAFD LKAHKRLGFN AVRKHIKVES
     PRWFHHADRL GLLVWQDFVS GDLTSDTGRA AFVDQGLETV RQHRSSPSVI GWVVFNEGWG
     EWNREESGRL AETVKAADPS RVVNAHSGVN CCNSKGDSGK GDIIDHHDYN NDDPPFPDHR
     AAMDGEHGGF TLRTPGHMWP GAPTVIYSGV EDKEALTRTY VENTEKYYLD QAAHELSGSV
     YTQITDLENE LNGLYTYDRR QIKVDPVRVR EINLRVIAAG AAAGERGNLE GGGHWALDEG
     TGGTARDDGP NGEPLTLTGG TTWTAGIDGS ALRFDGRGQY ARTDGPVLDT TAGYSVSAWV
     TLDSLPENYA TAVSQDTRRR AGPFYLQYGR GAFAFSTPGE HRARLEITPE TGRWYHLVGV
     RDSASDEIRL YVDGVPAATA KAGPAYPSTG PFTVGRAQWD GAHADFWDGA VDEVHAFDRA
     LTAAEVSALH ARQKP
//