ID K6T1X8_9CLOT Unreviewed; 357 AA.
AC K6T1X8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Beta-glucanase/beta-glucan synthetase {ECO:0000313|EMBL:EKQ53163.1};
GN ORFNames=A370_03850 {ECO:0000313|EMBL:EKQ53163.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ53163.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ53163.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC {ECO:0000256|ARBA:ARBA00006865}.
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:EKQ53163.1}.
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DR EMBL; ALXI01000117; EKQ53163.1; -; Genomic_DNA.
DR AlphaFoldDB; K6T1X8; -.
DR STRING; 1196322.A370_03850; -.
DR PATRIC; fig|1196322.3.peg.3762; -.
DR eggNOG; COG2273; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR Proteomes; UP000001325; 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 CDD; cd08023; GH16_laminarinase_like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR PANTHER; PTHR10963:SF55; GH16 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF19127; Choline_bind_3; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51170; CW; 2.
DR PROSITE; PS51762; GH16_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001325};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 24..269
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT REPEAT 299..318
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 319..338
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
SQ SEQUENCE 357 AA; 41381 MW; 36DFBD2E4E69B99E CRC64;
MKLSKLSLIA TALFLINNIQ FKSLEAYAQT TPDKWDLTWS DEFDGSEINS SNWTYDIDGH
GWGNNELEYY TNRPENARIE DGNLVIEARK ESYNGSQYTS ARLKSEGLQN FLYGKVEARM
KLPEGQGFWP AFWMLGSNMA SVKWPDCGEI DIMEHINDAK NVLGTLHWNA HNGNMYESHG
GQTNIDVSQY HNYSIEWSPN YIKWFVDDNE YFEYDITNNV NGTESLHKPF FIVLNLAVGG
NLPQNPDAST NFPAKMYVDY VRVYNRHSDS ISISKPRNAW YKDKSNGYNY YLDGDGNPYK
GWLYLKDYWY YLDSDGKMKT GWLNDSGNWY YLNEQGIMLK NTTIDGYTLD SNGVWIY
//
