ID B1VLN6_STRGG Unreviewed; 1098 AA.
AC B1VLN6;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Putative hydrolase {ECO:0000313|EMBL:BAG23427.1};
GN OrderedLocusNames=SGR_6598 {ECO:0000313|EMBL:BAG23427.1};
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG23427.1, ECO:0000313|Proteomes:UP000001685};
RN [1] {ECO:0000313|EMBL:BAG23427.1, ECO:0000313|Proteomes:UP000001685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX PubMed=18375553; DOI=10.1128/JB.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009493; BAG23427.1; -; Genomic_DNA.
DR RefSeq; WP_012382061.1; NC_010572.1.
DR AlphaFoldDB; B1VLN6; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GeneID; 6215905; -.
DR KEGG; sgr:SGR_6598; -.
DR PATRIC; fig|455632.4.peg.6771; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_009935_0_0_11; -.
DR Proteomes; UP000001685; 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 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAG23427.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1098
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039315820"
FT DOMAIN 55..199
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 310..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 119403 MW; C8034D5D54B76B32 CRC64;
MRRQHPRPRA LFRALTCAAA LLVPVGALLV PTAAAAPAVP AEAAERTFTA DDPVTDVHGL
KGEYFSMSAP GARDFAELGA TSLDPEINFP GLTGTFESAT GRTEHTTARW TGQLEAPETG
DYTFSAIGDN GFRLHLDGNV VIDHWEPDWD KEQHSAPISL KAGEKHAFKL EMFQDTGGAS
MFLRWEADGL KKQIVPESAF TPPADFEVYP VALGIAKNGK RLQATFRDRV ADWRKVKEHL
KIEVDTSPMP VKSVNRASDN PRALIIDLAA PVLKDQRVKV VYDGKGGLKS GAETVPEIGR
TAKNLSTHRL TTPWGDKLDK NHPLPEYPRP QQVRDQWKNL NGPWEFAGAA EGEQPVFGKK
LDEKIIVPFP VESQLSGLER DEDHMFYRKL VTVPKNWSIG KGGKGASGEG KRLKLNFDAV
DYRSTVWVNG TKVAEHTGGY TGFTADITDA LLGSGPQEIV VAVTDRTGPN QPKGKQSTNP
GGIVYTPTSG IWQTVWMEPV APAAIDSLTT TPDIDTGRLA VTVNSDKASA DARITAVARD
RKGKVVGTVS GPANRKLGLQ LTNQHLWSPD DPYLYDLDVS LTDGRSKDSV ESYFGMRQLK
VDKVGGYQKL VLNGKPFFSL AMLDQGFWPD GLYTQPSDAA LTFDLKAQKD LGFNAVRKHI
KVESPRWYYH ADRLGLLVWQ DFVNADIDND AGKNAFLTQG KELMKQFHNY PSISGWIVFN
EGWGEWDRTE TGKIAEDVKA LDPSRVVNAH SGVNCCASKG DSGKGEIIDH HDYVNNDPAF
PDDRRAAMDG EHGGFTLRTP GHMWPGAPAN IYSGVADKAA LTAKYVDNTR TYYLAAAGAE
LSGSVYTQVS DLENELNGLW TYDRREIKVD PKKVREINRQ VIAAGAAAGE RDELKGGGSW
SLDENTGTTA RDSGPNKAHL TLEGGSSWVP GVTGSALTFD GEGQYAQSSG PVVDTTKDYT
VSAWASLDAL PGNYATVVSQ DGRRTENPFY LQYGQGAFAF STPGGKRARW EITPETGKWY
HLVGVRKGDE ITLYVDGKPA ATTAAGPADV STGPLSVGRA QYDGARGDFW NGSVDQVGVY
DKALTAEEVS ALHGRQRP
//
