ID A5I0S4_CLOBH Unreviewed; 530 AA.
AC A5I0S4; A7G2I6;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:CAL82635.1};
GN OrderedLocusNames=CBO1081 {ECO:0000313|EMBL:CAL82635.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL82635.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL82635.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
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; AM412317; CAL82635.1; -; Genomic_DNA.
DR RefSeq; WP_003356323.1; NC_009698.1.
DR RefSeq; YP_001253612.1; NC_009495.1.
DR RefSeq; YP_001387001.1; NC_009698.1.
DR AlphaFoldDB; A5I0S4; -.
DR CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GeneID; 5185336; -.
DR KEGG; cbh:CLC_1134; -.
DR KEGG; cbo:CBO1081; -.
DR PATRIC; fig|413999.7.peg.1076; -.
DR HOGENOM; CLU_019399_0_2_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008843; F:endochitinase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 2.
DR CDD; cd06543; GH18_PF-ChiA-like; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR42976; BIFUNCTIONAL CHITINASE/LYSOZYME-RELATED; 1.
DR PANTHER; PTHR42976:SF1; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..530
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039549809"
FT DOMAIN 58..354
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 369..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 57569 MW; 3565EB71EAFE5945 CRC64;
MKSKKLTALV LSVLVASGAT SAILTEKNIV QAKEVKISSV QSKIATNIGI GEESWGSTVF
APYVDACSYP VFSLTEYAKE TGTKHFILGF IVDKNGQPSW GTYYDMEEGP TDYQGGGLLK
EIKALRQMGG DVMVSFGGEA NTPLAASIKD VNKLKDAYKK VIKDYGLTHI DFDIEGAWTA
DAASIERRSQ AIALLQKELK AENHPLKIWY TLPVLPSGMT NGVDVVKSAV KNGVELSGVN
VMTMCFGQKA PDGTMGDLVV ESAKSVHKQL KDIYTQANIQ KSDKEIWKMI GVTPMNGLDY
SGSILDQNGA RKVASFGKTV GMGLIGMWSV NRDYQNPKGS TNYVSITDSS ILQEKFEFGK
ILSNYDSNDG SGIIEKPGTT DPENPGDGEG GGEVEGVPAY KPQQEYSAGD KVSYKGKIYQ
AKWWTKGFAP DTAVQNSWDT PWELIGNSDD GKDVEDGKDV EDGKDVEDGK DIEDGGEVGS
APAYNLQQEY WGGDKVSYKG KVYQAKWWTK GFAPDTVVEN TWDTPWALIG
//