ID W4B726_9BACL Unreviewed; 479 AA.
AC W4B726;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN ORFNames=C161_05126 {ECO:0000313|EMBL:ETT39543.1};
OS Paenibacillus sp. FSL R5-192.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT39543.1, ECO:0000313|Proteomes:UP000019041};
RN [1] {ECO:0000313|EMBL:ETT39543.1, ECO:0000313|Proteomes:UP000019041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT39543.1,
RC ECO:0000313|Proteomes:UP000019041};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT39543.1}.
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DR EMBL; ASPR01000008; ETT39543.1; -; Genomic_DNA.
DR RefSeq; WP_036668556.1; NZ_ASPR01000008.1.
DR AlphaFoldDB; W4B726; -.
DR PATRIC; fig|1226754.4.peg.1046; -.
DR Proteomes; UP000019041; 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 CDD; cd10954; CE4_CtAXE_like; 1.
DR Gene3D; 3.30.565.40; Fervidobacterium nodosum Rt17-B1 like; 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 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 282..459
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 479 AA; 53665 MW; D9504616ED44F6CB CRC64;
MNKRKKTRWP VWLVGFIVLA GGILGINLMV QNVLAGNHSV TENVEVSPSA YPGLNIETRT
KNTKHYILSI SNVLTNSKEI NTPIQTWVND QEKKFLTQVK TGAKTLQGDY RAELNITVDT
NKISDHLYSL VFTSYQITAG SANGQSIIKS FNIDTAENKI LNLSDIMTYD KAAVNHIMSI
VKGELKKQKN VHSYVFEAEL QKSIKNPSGW KWSIGNGVFT LYFNKYEIAA GAAGTVQVNI
PLKSLHSYLK KDLTKKWNIT YENNDEPKGK RPTQPPLDPK GKYVALTFDD GPHPKVTPRV
LKTLKEYNAK ATFFMLGVQV EYYPDMAKKV AKAGHEIGNH SKSHPNLANM SLSEVRKQII
ESSHRIKDAT GEKPTLFRPP YGAMNESVKK VTKEQKTPII LWSVDSLDWK SRNAQAVNKE
VAKNIRSGSI VLMHDIHTST ADALPRMLKS LKKQGYQFVT VSQLLSLNES TGNGPYYNQ
//
