ID D9SM97_CLOC7 Unreviewed; 227 AA.
AC D9SM97;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN OrderedLocusNames=Clocel_4091 {ECO:0000313|EMBL:ADL53753.1};
OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL53753.1, ECO:0000313|Proteomes:UP000002730};
RN [1] {ECO:0000313|EMBL:ADL53753.1, ECO:0000313|Proteomes:UP000002730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC {ECO:0000313|Proteomes:UP000002730};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Clostridium cellulovorans 743B.";
RL Submitted (AUG-2010) 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};
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DR EMBL; CP002160; ADL53753.1; -; Genomic_DNA.
DR RefSeq; WP_010074102.1; NC_014393.1.
DR AlphaFoldDB; D9SM97; -.
DR STRING; 573061.Clocel_4091; -.
DR KEGG; ccb:Clocel_4091; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_021264_0_1_9; -.
DR OrthoDB; 9806342at2; -.
DR Proteomes; UP000002730; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd10959; CE4_NodB_like_3; 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 PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002730};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..222
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 227 AA; 26166 MW; 7D94E826F4D05D74 CRC64;
MSKVYSVVVA FILVYAILPN IYFRLFSHQV LKRAATKKKI VALTFDDGPD PRYTPELLNV
LRKNNVKCTF FVLAENALKY PELIKSIKDD GHYIGLHSLR HINAIVESPK KTRNTFLKSI
SIMEKLGVKI TLFRPPWGMV NLSTMFYTRT NHFKPILWST HSYDWIGWNT VENIKSLLLK
RIRPGDIVLL HDGRGKNNAP KRTIAALETV IPKLKKEGYE FVLVKDL
//
