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Database: UniProt
Entry: A0A269W5V4_9BACL
LinkDB: A0A269W5V4_9BACL
Original site: A0A269W5V4_9BACL 
ID   A0A269W5V4_9BACL        Unreviewed;       482 AA.
AC   A0A269W5V4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   ORFNames=CHH75_09220 {ECO:0000313|EMBL:PAK53669.1};
OS   Paenibacillus sp. 7541.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2026236 {ECO:0000313|EMBL:PAK53669.1, ECO:0000313|Proteomes:UP000215741};
RN   [1] {ECO:0000313|EMBL:PAK53669.1, ECO:0000313|Proteomes:UP000215741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7541 {ECO:0000313|EMBL:PAK53669.1,
RC   ECO:0000313|Proteomes:UP000215741};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (AUG-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};
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:PAK53669.1}.
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DR   EMBL; NQLZ01000015; PAK53669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A269W5V4; -.
DR   Proteomes; UP000215741; Unassembled WGS sequence.
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; 2.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 2.
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; 2.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 2.
DR   PROSITE; PS51677; NODB; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000215741}.
FT   DOMAIN          60..239
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   DOMAIN          285..466
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   482 AA;  53399 MW;  D63BBB51A377BFF4 CRC64;
     MFSGFRFLIL LTIIPVFGGC SLLGHPSGTI KGEVKAPAPA VERYEGDKSR EISYVYTARK
     ELSLTFNGMG DQKTMTALLD ELDAHGVKAT FFLPGVRVAE EPDIAKEIAA RGHEIENNTL
     NQLDMSTLDY DGIYKEIQLA NEVIERETGV KPRYVRTRSG DYPEDVPLAA AHLGMKAVVS
     YKINPRDRDM QSAEEIGEYV ARYMTRGGII SMNTDINPEV VAAVKYIAQA AEDIGYRLIT
     LDELVENGGE RKPLASIPGY DAAKINPDYH DAAYELVYKA RTDRKEVALT FDDFGSDKTV
     TQILDILEEH DVQVTFFLRA KGVEDNPNLA RAMLEGGHDV ANHTYSHPVV TTLTPEELQE
     DVVKAHQVIT EAIQEQPVML FRPPTGVVDD LRAKAIAATG YPIMAMYDVT TLDWDTSNTA
     DDIVNGIMTK TEEGSVILLH MLDGLHTIEA LPRVLTGLKD KGYTFVKMAD MIEHQSGARE
     RN
//
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