ID A0A1U7EE27_9LACT Unreviewed; 510 AA.
AC A0A1U7EE27;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN ORFNames=BW721_10500 {ECO:0000313|EMBL:APZ50021.1};
OS Jeotgalibaca sp. PTS2502.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Jeotgalibaca.
OX NCBI_TaxID=1903686 {ECO:0000313|EMBL:APZ50021.1, ECO:0000313|Proteomes:UP000187137};
RN [1] {ECO:0000313|EMBL:APZ50021.1, ECO:0000313|Proteomes:UP000187137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTS2502 {ECO:0000313|EMBL:APZ50021.1,
RC ECO:0000313|Proteomes:UP000187137};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; CP019433; APZ50021.1; -; Genomic_DNA.
DR RefSeq; WP_076768418.1; NZ_CP019433.1.
DR AlphaFoldDB; A0A1U7EE27; -.
DR STRING; 1903686.BW721_10500; -.
DR KEGG; jep:BW721_10500; -.
DR OrthoDB; 9812065at2; -.
DR Proteomes; UP000187137; 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; cd10917; CE4_NodB_like_6s_7s; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR Gene3D; 3.90.640.20; Heat-shock cognate protein, ATPase; 1.
DR InterPro; IPR021729; DUF3298.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR037126; PdaC/RsiV-like_sf.
DR PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR Pfam; PF11738; DUF3298; 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:UP000187137};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 311..488
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 270..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..290
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 57308 MW; F9A18419D6F32EF7 CRC64;
MEKLTTRGKI FFSLLALIIL IVGFTLPSFF KADVPNTEEP ETPDEPDSTE IEQVEVAESN
YPGLHLEIQT ADTDTYHYAI HSLTTDSEPL TETIQTWLTN KKETFIANVK EFANSERPAD
LNITLEMLPL SETMYNIIFN VYEINGGANG ISEAKTFVIN IAEDKMYTLY DFLHIENENH
TAFQELIRNK LNADENLQQN LREDALTDSL KQIDQLQWTI TKDALTIYWD KYEIAIGAVG
NIQIEVPLAE IEHLLTTTAH DILQIEVVEE PETSVEQEEQ EPEEPEDQEP SGEIATVPTP
PPSAGPQVDG KYVAITFDDG PHPKVTEQVL ETLRTFNAKA TFFMLGNQVD FYPNLVQQVA
QEGHEVGTHS QTHADLTVIG QDQLQNEFAF TNERIKDIIG YYPTQFRPPY GAYNSSVINQ
AVNYGQKIIM WSVDSLDWQS QDPVAINQMV TSQTVPGSII LLHDIHDATA QALPTILTNL
QNQDYTFVTV SQLLELQGAT GVGPHFGNYK
//
