ID A0A3P1S8V9_9FIRM Unreviewed; 443 AA.
AC A0A3P1S8V9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN ORFNames=EII25_03095 {ECO:0000313|EMBL:RRC92672.1};
OS Erysipelotrichaceae bacterium OH741_COT-311.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=2491058 {ECO:0000313|EMBL:RRC92672.1, ECO:0000313|Proteomes:UP000270315};
RN [1] {ECO:0000313|EMBL:RRC92672.1, ECO:0000313|Proteomes:UP000270315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH741_COT-311 {ECO:0000313|EMBL:RRC92672.1,
RC ECO:0000313|Proteomes:UP000270315};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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:RRC92672.1}.
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DR EMBL; RQZE01000005; RRC92672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1S8V9; -.
DR OrthoDB; 9812065at2; -.
DR Proteomes; UP000270315; Unassembled WGS sequence.
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 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:UP000270315};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 242..420
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 443 AA; 51410 MW; EB7F39A77690500E CRC64;
MYRRRRRRVR VDRIFKALIA LGFVFALAFG ALYYLSNYHF IPKQLIVDNQ SSKLKDLSPK
NASVLYYDSS FKKYDIDYEG MFKTLKEHPG SEGRNMRLGQ YEVKDINENY KEIKYKLSVN
NEVVNTYSFV IDKNTDSVLK EDIFGENIYK YVSGYIRSTL KQQHSDDDYY FSKDFYLKTD
YESIQIDGYR FADDKVYIQN NEFNMEIPVD LNVYGSDLNI DLGYTSNVLV KQYPRFVDPN
RKILCLTFDD GPHDTFTNEL LRELERYDGS ATFYMVGRRA NNEKGHKVIF DVLNAGSEVG
NHSYTHASLV KLSGDALEKE VYQFSRDVEQ LTNGEYKVKT YRVPYGAFSP ALKEYMEYPI
IQWNVDPEDW KARDIEVVKQ RILEGAKDGG IIVLHDIHPE TKQAVLDLIP TLIDEGYQLA
SVVSAADARG IPLEAHKVYY GLK
//
