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Database: UniProt
Entry: A0A1B1MKQ9_STRLN
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ID   A0A1B1MKQ9_STRLN        Unreviewed;       946 AA.
AC   A0A1B1MKQ9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Secreted cellulase {ECO:0000313|EMBL:ANS69190.1};
GN   ORFNames=SLINC_6966 {ECO:0000313|EMBL:ANS69190.1};
OS   Streptomyces lincolnensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS69190.1, ECO:0000313|Proteomes:UP000092598};
RN   [1] {ECO:0000313|EMBL:ANS69190.1, ECO:0000313|Proteomes:UP000092598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS69190.1,
RC   ECO:0000313|Proteomes:UP000092598};
RA   Meng S.C.;
RT   "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT   actinobacteria.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP016438; ANS69190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B1MKQ9; -.
DR   STRING; 1915.SLINC_6966; -.
DR   KEGG; sls:SLINC_6966; -.
DR   PATRIC; fig|1915.4.peg.7677; -.
DR   Proteomes; UP000092598; Chromosome.
DR   GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.170.160.10; Endo-1,4-beta-glucanase f. Domain 2; 1.
DR   Gene3D; 4.10.870.10; Endo-1,4-beta-glucanase f. Domain 3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR023309; Endo-1-4-beta-glucanase_dom2.
DR   InterPro; IPR027390; Endoglucanase_F_dom3.
DR   InterPro; IPR000556; Glyco_hydro_48F.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF17957; Big_7; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF02011; Glyco_hydro_48; 1.
DR   PRINTS; PR00844; GLHYDRLASE48.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51173; CBM2; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092598};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          9..119
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
SQ   SEQUENCE   946 AA;  100290 MW;  B22E4232AE4B7841 CRC64;
     MLSTGSTPAQ AAAVQCSVDY KTNDWGSGFT VDVTITNRGT DTIAGWNLAY GYTGNQKLSG
     TGWNGTWSQS GQAISVRNAA HNATIAAGAA VSTGAQFSYS GTNTAPTAFS VNGTACNGAH
     QPPIAVLTSP AAGAVYTQGS AVPLAATAAA ADGATISKVE FYDDTTLLGT DTSSPYSLSA
     SGLTVGSHSL VAKAYDSLGA SASSTPVGIT VASGPAVVAS TNQLAVQQGK TGTFDVKLST
     QPSANVTVTT ARSGGNTGLS VTGGASLTFT PSNWNTAQRV TITANASGSG AATFDSTATG
     HAKSTVTVTQ IAAAGEYDAR FLEMYGKITN PANGYFSPEG IPYHSVETLI VEAPDHGHET
     TSEAYSYLLW LQAMYGKVTG DWTRFNGAWE IMEKYMIPTR ADQPTNSFYN ASKPATYAPE
     LDTPNQYPAP LDTSVPVGRD PIAGELKSAY GTDDIYGMHW LQDVDNIYGY GNSPGKCEAG
     PTDTGPSYIN TFQRGAQESV WETVPQPTCD AFKYGGKNGY LDLFTGDASY AKQWKFTNAP
     DADARAVQAA YWADKWADAQ GKGGEISATV GKAAKMGDYL RYSMYDKYFK KIGNCVGPSA
     CPAGTGKDAS MYLMSWYYAW GGATDTSAGW SWRIGSSHAH GGYQNPLAAY ALSSYADLKP
     KSATGQADWA KSLDRQLEFY RWLQSNEGGI AGGATNSWAG RYATPPAGKS TFYGMYYDQQ
     PVYHDPPSNQ WFGFQAWSME RVAEYYQQTG DADAKVVLDK WVDWALAHTT INPDGTFRIP
     STLQWSGQPD TWNASSPGSN SGLHVTVADY TNDVGVAAAY AKTLTYYADR SGDTQAASTA
     KALLDGMWDN HQDALGVAVP ENRADYNRFD DPVSVPSGWT GTMPNGDAIN SSSTFDSIRS
     FYEDDPAWSK IEAYLAGGAV PSFTYHRFWA QADIALAMGS YAELLE
//
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