ID A0A0X1RW76_9BACL Unreviewed; 456 AA.
AC A0A0X1RW76;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN ORFNames=ASO14_2658 {ECO:0000313|EMBL:AMA62759.1};
OS Kurthia sp. 11kri321.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA62759.1, ECO:0000313|Proteomes:UP000058129};
RN [1] {ECO:0000313|EMBL:AMA62759.1, ECO:0000313|Proteomes:UP000058129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11kri321 {ECO:0000313|EMBL:AMA62759.1,
RC ECO:0000313|Proteomes:UP000058129};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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};
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DR EMBL; CP013217; AMA62759.1; -; Genomic_DNA.
DR RefSeq; WP_068456251.1; NZ_CP013217.1.
DR AlphaFoldDB; A0A0X1RW76; -.
DR STRING; 1750719.ASO14_2658; -.
DR KEGG; kur:ASO14_2658; -.
DR PATRIC; fig|1750719.3.peg.2617; -.
DR OrthoDB; 9812065at2; -.
DR Proteomes; UP000058129; Chromosome.
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 Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR Gene3D; 3.90.640.20; Heat-shock cognate protein, ATPase; 1.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000058129};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 267..441
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 456 AA; 51427 MW; 29D39519BA9A517B CRC64;
MKSSPFKNRL LIDSLLVCIL LSLIIFAVVY MLNLKSPSEK GLAASTENTS TAETDNPFIK
TVTVTNETEQ GSYTIQYPKT GSSELNTAIS DAVKEMKTDF FKGKYAKDAQ MHVTYMTLKH
KDLYSFVLTQ SLQEDKQKKD QKFITFTVDQ PANELIDIKE VIPSGEQLTH IMNLSQKELA
KHKEVQNFNK SQQKDLAINQ EASHFENFAL DDQNLYFYLN PDSFTSSFNQ PITITLPLQN
INSSLAKEFQ IPVKKIIQKK KKPIPKKAVA LTFDDGPNTT STKSILATLK REKVKATFFM
VGTQARANPK MVKQIADEGH ELGNHSLTHA NLVLLSNANV KKEIETTNQA IKKATGKNPT
VFRPPYGSYN ANVSKIAKMP VVLWNVDTLD WKHHNPQQTL ANVKSQKSQY TTVLMHDIHA
SSAQALPQVI RYLKQQGYTF VTASEMLSIE KRVYKK
//
