ID C9ZEC5_STRSW Unreviewed; 485 AA.
AC C9ZEC5;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative secreted glycosyl hydrolase {ECO:0000313|EMBL:CBG74916.1};
GN OrderedLocusNames=SCAB_79561 {ECO:0000313|EMBL:CBG74916.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG74916.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG74916.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG74916.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|RuleBase:RU361153}.
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DR EMBL; FN554889; CBG74916.1; -; Genomic_DNA.
DR RefSeq; WP_013005366.1; NC_013929.1.
DR AlphaFoldDB; C9ZEC5; -.
DR SMR; C9ZEC5; -.
DR STRING; 680198.SCAB_79561; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR GeneID; 24311220; -.
DR KEGG; scb:SCAB_79561; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_044209_0_0_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR31297:SF41; ENDOGLUCANASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G01830)-RELATED; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:CBG74916.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..485
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003005724"
FT DOMAIN 355..477
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 485 AA; 52157 MW; C2F25713A99AFA7E CRC64;
MPRTRRRRYL ARALACILTV PSVPAAVAHE SAAPTPADTS QFRGVNWARL GDNFHAGPLV
LHGLSASDSY RTVLAKADAV YTGFEKNLGA NTVRLPINTY TVGTSWWNAY TGAIDAATAR
GFKVVLSYWD DGVAARGGRI VNPSAFDAMW NTVVARYGSD SLVHFEPMNE PAGHSAAEWA
NVASDWIAGR PSIPRNRIVV SGAGLNTDIT SMCADRRLDG TLLSLHHYTF FSGAKTYDQW
MAHLRNALGS CADRTIVDEF GAPMDTGLNY RDAGSTDNFV RYFRATTTVL RELRIGSVYW
PGLGGKIRAG QGDDWYAMQK LHGTGTDLTL STPSASGRER LRHGWGLDGD APAPAGPVRN
VGTGRCLDIP GGTTANIQVQ VTTCDDTVGQ QWTVTADGQI TALGGRRCMD AYNSGTTNGT
VVGTWACNGG DNQRWTVGGD GTVRSARSGL CLDVNTATFK AQLWACWGGD NQAWQIRKVS
DLPRS
//
