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Database: UniProt
Entry: F1Z1W7_9STRE
LinkDB: F1Z1W7_9STRE
Original site: F1Z1W7_9STRE 
ID   F1Z1W7_9STRE            Unreviewed;       425 AA.
AC   F1Z1W7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   ORFNames=SPB_0918 {ECO:0000313|EMBL:EGE53341.1};
OS   Streptococcus parauberis NCFD 2020.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=873447 {ECO:0000313|EMBL:EGE53341.1, ECO:0000313|Proteomes:UP000003732};
RN   [1] {ECO:0000313|EMBL:EGE53341.1, ECO:0000313|Proteomes:UP000003732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCFD 2020 {ECO:0000313|EMBL:EGE53341.1,
RC   ECO:0000313|Proteomes:UP000003732};
RA   Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA   Town C.D.;
RL   Submitted (FEB-2011) 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:EGE53341.1}.
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DR   EMBL; AEUT02000001; EGE53341.1; -; Genomic_DNA.
DR   RefSeq; WP_003102928.1; NZ_AEUT02000001.1.
DR   AlphaFoldDB; F1Z1W7; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_037608_1_0_9; -.
DR   Proteomes; UP000003732; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.640.30; -; 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   SUPFAM; SSF144015; Peptidoglycan deacetylase N-terminal noncatalytic region; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        5..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          242..416
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   425 AA;  48776 MW;  10FBE3C1378C7930 CRC64;
     MRKVFYTLIG FLGIILITSG LFFWKSWSIQ NDLVKIIKNE NINNLTENSF LSKKIIHRKN
     QTYYYFAPTA INKDFYHENL PSSVYKSTQK DQYVFLKPEF STTDLKGVKN VKIHKIVYEA
     GFLKLKRVSD HVVSDYHIKT DYQTFHLSEL VSGHLDDITR IVTKDYPDQK FEISDYSQIS
     EENGILRDHF KVKDKILIID KTIQVPLQEL FDVIDSNFLT GQSKIDFTEY QKAKEAALHP
     KKLVALTFDD GPNPLTSPQV ISILQKYNAK ATFFMMGSKV LGNESILKSV IASGSEIGNH
     TWDHPYLTKQ SDEEVKSQIE RTNIAIEKAC GKRPIYLRPP YGATNARVEK LSGMTEILWT
     VDTRDWENHN TEKIMANIKS QLHPGGIILM HDIHQTSLQA LPTVLDYLKK EGYQCVTVSK
     LLGDN
//
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