ID A0A943QHA2_CLOSP Unreviewed; 857 AA. AC A0A943QHA2; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 24-JUL-2024, entry version 7. DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052}; DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052}; GN ORFNames=KIC62_06345 {ECO:0000313|EMBL:MBS5937972.1}; OS Clostridium sp. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1506 {ECO:0000313|EMBL:MBS5937972.1, ECO:0000313|Proteomes:UP000778803}; RN [1] {ECO:0000313|EMBL:MBS5937972.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L3_069_061G1_dasL3_069_061G1_concoct_30_sub RC {ECO:0000313|EMBL:MBS5937972.1}; RA Lou Y.C.; RT "Infant gut strain persistence is associated with maternal origin, RT phylogeny, and functional potential including surface adhesion and iron RT acquisition."; RL Submitted (FEB-2021) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D- CC glucosamine + acetate.; EC=3.5.1.104; CC Evidence={ECO:0000256|ARBA:ARBA00043715}; 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:MBS5937972.1}. 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; JAHAIX010000006; MBS5937972.1; -; Genomic_DNA. DR Proteomes; UP000778803; Unassembled WGS sequence. DR GO; GO:0005628; C:prospore membrane; IEA:TreeGrafter. DR GO; GO:0004099; F:chitin deacetylase activity; IEA:TreeGrafter. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd10917; CE4_NodB_like_6s_7s; 3. DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 3. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR002509; NODB_dom. DR InterPro; IPR050248; Polysacc_deacetylase_ArnD. DR PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1. DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1. DR Pfam; PF01522; Polysacc_deac_1; 3. DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 3. DR PROSITE; PS51677; NODB; 2. PE 4: Predicted; KW Membrane {ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 5..24 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 73..259 FT /note="NodB homology" FT /evidence="ECO:0000259|PROSITE:PS51677" FT DOMAIN 655..850 FT /note="NodB homology" FT /evidence="ECO:0000259|PROSITE:PS51677" FT REGION 311..330 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 857 AA; 96613 MW; 94A58A50C26134C5 CRC64; MKKKVYWIGL CIVLLSVFFI SLYFKFIEKS PLNTDITAIN SNYDTSKKIK LALKDYNKDK KAEIISSFDT KENIIAISFE GIRNNEITKE VLSLLNKYNV KSTFFASGVE AAEDSDLINS IEKNGHSIGS LGLSDKKHME ELTKDELITD FTKANKVLES ITGNTSLLLK SSSTIYNDTV LASAYASGNK FVVDSKNYLS YQSFKNYEEA QGYVKSLKKG EIVSVKLEGV LDESEYTKKE EKPAIDKEDG IEKKDEEIIK YASILEVVEW LCQAINEDGR TTVLLDNYNY LEKSDERTMF IRNDFISNNS LNSNPSNNNS GNSNLGDDGS EDNSIDLSNI NFNKLIKANK NLLAENISRF YTTQEAVAYT FRGISDKESL NLMLAALSIT NTKGTFFVSK KEILEYPDRI EKILSYGNEI GNGGVTANSD ILNKSAEEIA KEIYEVDKML KDRGIYTNAY MSGFGYSDSE IREAVSAVRN IEGLGKYELI TYSKAPIISK YEGKDSDYIL NDYLNPDIYT SLSKGEIVYF RLDSGLVDQK VIYELMIGIT FKYVNFGYAK MYDASIGDYK LRSKPLGYSV VTISNLQNNY EGESGYGRYE LLINSHSLQR KSMEEALNLV NERYIGNEFV ELDGFTEEEK SRLDQEGTID TNGEDVIFFT FDDWGGDTIV NEILDVLDKH KVKGSFFTIS KYIDDNSGIS NSNPNLLRTI ALKGHDIGSH NYNHEILEED KNLLIDSLGK SYDSMANVIG DLDSLKPYFR PPTLYVNKDG LLAVFESGFD YSISGNISTH DYEATSPIEI INNFESQLQD GKGNIVVMHM NNQSYYTAMA LDIFLTNNEN GLYGKKYKIA KLSDYLK //