ID Q5WDB3_SHOC1 Unreviewed; 430 AA. AC Q5WDB3; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 04-NOV-2026, entry version 107. DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:BAD65647.1}; GN OrderedLocusNames=ABC3113 {ECO:0000313|EMBL:BAD65647.1}; OS Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Shouchella. OX NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD65647.1, ECO:0000313|Proteomes:UP000001168}; RN [1] {ECO:0000313|EMBL:BAD65647.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD65647.1, RC ECO:0000313|Proteomes:UP000001168}; RA Hakamada Y., Kobayashi T., Hitomi J., Kawai S., Ito S.; RT "Molecular cloning and nucleotide sequence of the gene for an alkaline RT protease from the alkalophilic Bacillus sp. KSM-K16."; RL J. Ferment. Bioeng. 78:105-108(1994). RN [2] {ECO:0000313|EMBL:BAD65647.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD65647.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=7632397; DOI=10.1007/s002530050437; RA Kobayashi T., Hakamada Y., Adachi S., Hitomi J., Yoshimatsu T., Koike K., RA Kawai S., Ito S.; RT "Purification and properties of an alkaline protease from alkalophilic RT Bacillus sp. KSM-K16."; RL Appl. Microbiol. Biotechnol. 43:473-481(1995). RN [3] {ECO:0000313|EMBL:BAD65647.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD65647.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=9278275; DOI=10.1093/protein/10.6.627; RA Shirai T., Suzuki A., Yamane T., Ashida T., Kobayashi T., Ito S.; RT "High-resolution crystal structure of M-protease: phylogeny aided analysis RT of the high-alkaline adaptation mechanism."; RL Protein Eng. 10:627-634(1997). RN [4] {ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168}; RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM- RT K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:BAD65647.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD65647.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=17429572; DOI=10.1007/s00792-007-0074-1; RA Kageyama Y., Takaki Y., Shimamura S., Nishi S., Nogi Y., Uchimura K., RA Kobayashi T., Hitomi J., Ozaki K., Kawai S., Ito S., Horikoshi K.; RT "Intragenomic diversity of the V1 regions of 16S rRNA genes in high- RT alkaline protease-producing Bacillus clausii spp."; RL Extremophiles 11:597-603(2007). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. CC {ECO:0000256|PROSITE-ProRule:PRU01258}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01258}. 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; AP006627; BAD65647.1; -; Genomic_DNA. DR RefSeq; WP_011247955.1; NC_006582.1. DR STRING; 66692.ABC3113; -. DR PaxDb; 66692-ABC3113; -. DR KEGG; bcl:ABC3113; -. DR eggNOG; COG1388; Bacteria. DR eggNOG; COG3858; Bacteria. DR HOGENOM; CLU_037415_4_1_9; -. DR OMA; ADAIMIM; -. DR OrthoDB; 9769314at2; -. DR CDD; cd02874; GH18_CFLE_spore_hydrolase; 1. DR CDD; cd00118; LysM; 2. DR Gene3D; 3.10.50.10; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 3.10.350.10; LysM domain; 2. DR InterPro; IPR041704; CFLE_GH18. DR InterPro; IPR011583; Chitinase_II/V-like_cat. DR InterPro; IPR029070; Chitinase_insertion_sf. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR001223; Glyco_hydro18_cat. DR InterPro; IPR018392; LysM. DR InterPro; IPR036779; LysM_dom_sf. DR PANTHER; PTHR46066:SF2; CHITINASE DOMAIN-CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR46066; CHITINASE DOMAIN-CONTAINING PROTEIN 1 FAMILY MEMBER; 1. DR Pfam; PF00704; Glyco_hydro_18; 1. DR Pfam; PF01476; LysM; 2. DR SMART; SM00636; Glyco_18; 1. DR SMART; SM00257; LysM; 2. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF54106; LysM domain; 2. DR PROSITE; PS51910; GH18_2; 1. DR PROSITE; PS51782; LYSM; 2. DR GO; GO:0008061; F:chitin binding; IEA:InterPro. DR GO; GO:0070492; F:oligosaccharide binding; IEA:TreeGrafter. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Proteomes; UP000001168; Chromosome. DR AlphaFoldDB; Q5WDB3; -. PE 3: Inferred from homology; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE- KW ProRule:PRU01258}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01258}; Reference proteome {ECO:0000313|Proteomes:UP000001168}. FT DOMAIN 2..46 FT /note="LysM" FT /evidence="ECO:0000259|PROSITE:PS51782" FT DOMAIN 51..95 FT /note="LysM" FT /evidence="ECO:0000259|PROSITE:PS51782" FT DOMAIN 103..430 FT /note="GH18" FT /evidence="ECO:0000259|PROSITE:PS51910" FT ACT_SITE 218 FT /note="Proton donor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01258" SQ SEQUENCE 430 AA; 47888 MW; 5D4724B4FD50B64F CRC64; MQLHVVQAGE SLYGIAQAYS TSPQSIATAN QLDAPNELVV GQTLVIPIYG RYYFVQPGDT LSVIAARYGF SVQQLAEINN LMPTQVLPVG FRLYLPPAAK QEIETNAYIE PTQDTISEAL LTSAREAAPY LTYLAPFSYR ITAEGALLPV PLGSLPDIAD ENNTALMMVI TNLQEGAFSG ELGQTVLESP DIQNTLLDAI ITEANRVGRF SDVHFDFEFL PPAMREPYNA FLRKAVDRLH QEGLLVSTAL APKTSAAQTG QWYEAHDYRA HGDIVDFVVL MTYEWGYSGG PPQAVSPIGP VTEVVEYALT EMAPDKIMLG QNLYGYDWTL PFEPGGEYAR AISPQQAIAL AREHNVAIEF DTDAQAPFFH YIDANGREHE VWFEDGRSIQ AKFNLIKQNE LRGISYWKLG LSFPQNWLLL NDQFTIRKRR //