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Database: UniProt
Entry: R7ZI96_LYSSH
LinkDB: R7ZI96_LYSSH
Original site: R7ZI96_LYSSH 
ID   R7ZI96_LYSSH            Unreviewed;       470 AA.
AC   R7ZI96;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   ORFNames=H131_04099 {ECO:0000313|EMBL:EON73815.1};
OS   Lysinibacillus sphaericus OT4b.31.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1285586 {ECO:0000313|EMBL:EON73815.1, ECO:0000313|Proteomes:UP000013911};
RN   [1] {ECO:0000313|EMBL:EON73815.1, ECO:0000313|Proteomes:UP000013911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT4b.31 {ECO:0000313|EMBL:EON73815.1,
RC   ECO:0000313|Proteomes:UP000013911};
RA   Pena-Montenegro T.D., Dussan J.;
RT   "Draft genome of the heavy metal tolerant bacterium Lysinibacillus
RT   sphaericus strain OT4b.31.";
RL   Submitted (APR-2013) 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:EON73815.1}.
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DR   EMBL; AQPX01000008; EON73815.1; -; Genomic_DNA.
DR   RefSeq; WP_010857784.1; NZ_KB933398.1.
DR   AlphaFoldDB; R7ZI96; -.
DR   PATRIC; fig|1285586.5.peg.829; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_037608_3_0_9; -.
DR   Proteomes; UP000013911; 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:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
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   Carbohydrate metabolism {ECO:0000313|EMBL:EON73815.1};
KW   Glycosidase {ECO:0000313|EMBL:EON73815.1};
KW   Hydrolase {ECO:0000313|EMBL:EON73815.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000313|EMBL:EON73815.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Xylan degradation {ECO:0000313|EMBL:EON73815.1}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          286..460
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   470 AA;  53325 MW;  CE7A460CCA5B1ADE CRC64;
     MMQERRKRRG PMIDFLLIGL IIALTSIILV IILSKDDFKF QKISASKDSN SNSLNSNLST
     ESSAFPGIRI VTDVSNDKRT PFAIHYPQTE NKVFNDAVLQ YITDSKENYL SEMKKNNTKD
     AMGELNISFE TFPYQEHYYS FVLTKMQYLG GANHEVSTKT FFFNNETGEQ IDIKTLLQND
     ENNLSTIATH VRKDLQQNPQ LKVELNKDDL LTATEPKWAN FERFAIVKDA LLFYFDEYEI
     ANGAAGAPIV KLPLTLINPL LASDFQIAME TMEPTKPETP GDPNAKRIAL TFDDGPHPIV
     TEQILDILDK YHAKATFFML GSRVQYYPDI ARDVLARGHE IGNHTWNHPV LTKLSSEQVL
     KEYSSTAAEI ELAINQGATV FRPPYGATNN DINAQMPIPV VLWSIDTMDW KHRNAQQLLP
     YVKNNLHNNA IVLMHDIHQS TADGLDAVLA FLQEQGYEFV TVSEILPYRQ
//
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