ID Q5WIH1_SHOC1 Unreviewed; 259 AA. AC Q5WIH1; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 02-SEP-2026, entry version 100. DE SubName: Full=Polysaccharide deacetylase {ECO:0000313|EMBL:BAD63834.1}; GN OrderedLocusNames=ABC1296 {ECO:0000313|EMBL:BAD63834.1}; OS Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Shouchella. OX NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD63834.1, ECO:0000313|Proteomes:UP000001168}; RN [1] {ECO:0000313|EMBL:BAD63834.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63834.1, 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:BAD63834.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63834.1, 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:BAD63834.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63834.1, 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:BAD63834.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63834.1, 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 --------------------------------------------------------------------------- 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; BAD63834.1; -; Genomic_DNA. DR RefSeq; WP_011246147.1; NC_006582.1. DR AlphaFoldDB; Q5WIH1; -. DR STRING; 66692.ABC1296; -. DR PaxDb; 66692-ABC1296; -. DR KEGG; bcl:ABC1296; -. DR eggNOG; COG0726; Bacteria. DR HOGENOM; CLU_021264_12_1_9; -. DR OrthoDB; 9812065at2; -. DR Proteomes; UP000001168; Chromosome. DR GO; GO:0016020; C:membrane; IEA:TreeGrafter. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd10948; CE4_BsPdaA_like; 1. DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR002509; NODB_dom. DR InterPro; IPR050248; Polysacc_deacetylase_ArnD. DR InterPro; IPR014235; Spore_PdaA. DR NCBIfam; TIGR02884; spore_pdaA; 1. DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1. DR PANTHER; PTHR10587:SF78; PEPTIDOGLYCAN-N-ACETYLMURAMIC ACID DEACETYLASE PDAA; 1. DR Pfam; PF01522; Polysacc_deac_1; 1. DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1. DR PROSITE; PS51677; NODB; 1. PE 4: Predicted; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01014}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01014}; KW Reference proteome {ECO:0000313|Proteomes:UP000001168}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..259 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004263399" FT DOMAIN 66..247 FT /note="NodB homology" FT /evidence="ECO:0000259|PROSITE:PS51677" FT ACT_SITE 73 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01014" FT ACT_SITE 222 FT /note="Proton donor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01014" FT BINDING 74 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01014" FT BINDING 124 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01014" FT BINDING 128 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01014" SQ SEQUENCE 259 AA; 29409 MW; F54F0ECE7528FF67 CRC64; MKNAICLLLS LSIIIGQTSL ALGYENKTYN WSYKPAPAHT PADTEPMYKE LLEKADGYFI GDRDSKSLYL TFDNGYENGY TEKVLDVLKE KQVTGAFFVT GHYLKTAPEL VKRMVAEGHI VGNHSYHHPS LPQTSDAKLA AELDDVKTLF TEITGETEMR YLRPPRGEFS ERTLMKSKEL GYTNVFWSLA YKDWEVDKQK GGKYAYDQVM KRIHPGAIML IHAVSPDNAE ALPDIIDECR RQGYTFRSLD ELSLHSPMP //