ID G7LXC7_9CLOT Unreviewed; 517 AA.
AC G7LXC7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Glycoside hydrolase family 25 {ECO:0000313|EMBL:EHI96789.1};
GN ORFNames=CDLVIII_0047 {ECO:0000313|EMBL:EHI96789.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI96789.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHI96789.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI96789.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC {ECO:0000256|ARBA:ARBA00010646}.
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DR EMBL; CM001240; EHI96789.1; -; Genomic_DNA.
DR RefSeq; WP_009167475.1; NZ_CM001240.1.
DR AlphaFoldDB; G7LXC7; -.
DR STRING; 641107.CDLVIII_0047; -.
DR eggNOG; COG3757; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR HOGENOM; CLU_027326_0_0_9; -.
DR Proteomes; UP000005106; Chromosome.
DR GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06525; GH25_Lyc-like; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 4.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR002053; Glyco_hydro_25.
DR InterPro; IPR018077; Glyco_hydro_fam25_subgr.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34135; LYSOZYME; 1.
DR PANTHER; PTHR34135:SF2; LYSOZYME; 1.
DR Pfam; PF01473; Choline_bind_1; 4.
DR Pfam; PF19127; Choline_bind_3; 3.
DR Pfam; PF01183; Glyco_hydro_25; 1.
DR SMART; SM00641; Glyco_25; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 2.
DR PROSITE; PS51170; CW; 6.
DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHI96789.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005106};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..517
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003499304"
FT REPEAT 77..96
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 139..158
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 159..178
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 199..218
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 219..238
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 239..258
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 296..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 56891 MW; 6498FF5151E0C12B CRC64;
MNIKKKLAVL SVLTMFSLVP ALGVQAATAD ANITSTIGWK SENGAWYYYK PDNTKAVGWI
KPDNSWYYLK EDDGKMATGW IKDNGTWYYL DTSGAMATGW KLLNGDWYFL TGSGAMATGI
QNDGSNLYYL KDSGALATTT GWIKLNKKWY YINNGGKVAT GWITDNNKKY YLQTDGSMVT
GTNTIDGKAY TFNDSGDLKT GWIQSNNNWY YFDSNGNKVT GWVTLSGVKY YLKDDGTMAT
GWLSLNGSKY YLHDDGSMAT GWITLDGSDY YLDTTTGKML TNTTIDGYKI GADGKRTGTS
SLNTAPPPST NNSGGNTSSG STSNSSGQYY GIDISNYDGT IDFNAVKSSG VQLVYIKATE
GTTFIDPYLQ VNYSGASAAG LKTGFYHFLV GTSAPETQAD NFYNNIKDKR NDLKPMLDIE
STGFDVMDYT LRFIAEFKKV SNMNIGIYTY SSFISNLDGR LSTYPLWEAN YNNTPLQNLP
TNSVWFSRVG HQYSDTGYVT GISTDVDLDE FTGGIFS
//
