ID Q2RJL8_MOOTA Unreviewed; 241 AA.
AC Q2RJL8;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN OrderedLocusNames=Moth_1057 {ECO:0000313|EMBL:ABC19371.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC19371.1};
RN [1] {ECO:0000313|EMBL:ABC19371.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC19371.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL Submitted (DEC-2005) 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; CP000232; ABC19371.1; -; Genomic_DNA.
DR RefSeq; YP_429914.1; NC_007644.1.
DR AlphaFoldDB; Q2RJL8; -.
DR STRING; 264732.Moth_1057; -.
DR EnsemblBacteria; ABC19371; ABC19371; Moth_1057.
DR KEGG; mta:Moth_1057; -.
DR PATRIC; fig|264732.11.peg.1138; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_021264_0_2_9; -.
DR OrthoDB; 9806342at2; -.
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; cd10950; CE4_BsYlxY_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 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..232
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 241 AA; 26875 MW; D1A6C2097F90B2FF CRC64;
MYVFYWQRHG FKGWGFLAIL GLLLLLGFTC WRWFGRAAVP VMKTQPIYQG DPERKAIALT
FTIDWGEEYL PAILTALEQV GARATFFPTG QWAERHPELV RQMAAAGHEI GNHGQSHPHP
DNLSREENRQ DILQGEATLK AITGKKPVLY SPPYGESKPQ VVAAASDLGY KFIMWTINTG
DYLPNTQPED ILATILPKCQ NGAIVLLHPT EPAAKALPEL LKQLKERGYA LVTTSEILPN
G
//
