ID A0A081P602_9BACL Unreviewed; 296 AA.
AC A0A081P602;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN ORFNames=ET33_36720 {ECO:0000313|EMBL:KEQ26125.1};
OS Paenibacillus tyrfis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ26125.1, ECO:0000313|Proteomes:UP000028123};
RN [1] {ECO:0000313|EMBL:KEQ26125.1, ECO:0000313|Proteomes:UP000028123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSt1 {ECO:0000313|EMBL:KEQ26125.1,
RC ECO:0000313|Proteomes:UP000028123};
RA Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT "Draft genome sequence of Paenibacillus sp. MSt1.";
RL Submitted (JUN-2014) 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:KEQ26125.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JNVM01000008; KEQ26125.1; -; Genomic_DNA.
DR RefSeq; WP_036680739.1; NZ_JNVM01000008.1.
DR AlphaFoldDB; A0A081P602; -.
DR eggNOG; COG0726; Bacteria.
DR OrthoDB; 9806342at2; -.
DR Proteomes; UP000028123; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10917; CE4_NodB_like_6s_7s; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000313|EMBL:KEQ26125.1};
KW Glycosidase {ECO:0000313|EMBL:KEQ26125.1};
KW Hydrolase {ECO:0000313|EMBL:KEQ26125.1};
KW Polysaccharide degradation {ECO:0000313|EMBL:KEQ26125.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028123};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:KEQ26125.1}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..296
FT /note="peptidoglycan-N-acetylglucosamine deacetylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039536728"
FT DOMAIN 106..287
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 20..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 32369 MW; 6561DDF22DBFCA0B CRC64;
MSKQWIAILA ALLLLTSCGS KPDASPNAAA KTEPPASQPV SGGEKPKSAD GASVSNQPAP
SPAQEGKETV PADSVKKQEQ QVAKRYTMNP KTYDIVPIDP NGASKKVVLL TFDDGPKDLE
MNKALLDTLQ KHKAKAIFFL NGYRIKQKPE LVKLLASSGQ TIGNHSWDHI DLKKETKEKV
NQQIGDVQKA IKELTGKAPV FFRPPFGSGS DDVRAKAKEE GLLFMTWSNG SKDWEMTVKK
NSPEQVISNV LSQLHPGSNI LMHELPWTVE ALDKLLTQLE EKGYGFVNPE EIETTS
//