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Database: UniProt
Entry: A0A081P602_9BACL
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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}.
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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
//
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