ID W7YWV3_9BACL Unreviewed; 467 AA.
AC W7YWV3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, 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=JCM16418_837 {ECO:0000313|EMBL:GAF06854.1};
OS Paenibacillus pini JCM 16418.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1236976 {ECO:0000313|EMBL:GAF06854.1, ECO:0000313|Proteomes:UP000019364};
RN [1] {ECO:0000313|EMBL:GAF06854.1, ECO:0000313|Proteomes:UP000019364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16418 {ECO:0000313|EMBL:GAF06854.1,
RC ECO:0000313|Proteomes:UP000019364};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida Y., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Paenibacillus pini JCM 16418T, Isolated from the
RT Rhizosphere of Pine Tree.";
RL Genome Announc. 2:e00210-14(2014).
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:GAF06854.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAVZ01000002; GAF06854.1; -; Genomic_DNA.
DR RefSeq; WP_036646389.1; NZ_BAZT01000002.1.
DR AlphaFoldDB; W7YWV3; -.
DR STRING; 1236976.JCM16418_837; -.
DR eggNOG; COG0726; Bacteria.
DR OrthoDB; 2649545at2; -.
DR Proteomes; UP000019364; 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 CDD; cd10959; CE4_NodB_like_3; 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.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019364};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..224
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 467 AA; 53819 MW; 4FB01C102B1AB763 CRC64;
MQTLLLWLFY ISSFYAFIPG LITRIFGFRV FRRGTSEHEF ALTFDDGPDP VYTPKLLDLL
KRYDAKATFF VVGSHAEQHP ELVKRMYDEG HLIGIHNYVH KSNWLMRPAT VKKQIMKTDK
IIHSITGERT TYYRPPWGIV NLFDFAKKSQ FKIVLWSAMF GDWREKIGAD RLTERMLSKL
QPGVVMLLHD CGTTAGANLD APRQMLVALE RVLEEAGRLG LQSIRIDDMI EAKEKAPEKQ
LSRSKLATVK LWLMWDALFH MVFRLKTVHP ADPFLHYRYR SYQGAKVTMD NGEVISKGDK
VIELHFDNEK LFQMSLKSRS MVHLAIRMIR SMEHDLPSLA HQVMNDPKMS DARALYGVTM
INRGPQQFGF KVMDLEEGLF ARATRIYLKF LMLIIHPSGQ NRLKDHAELL VPKVLLMSMD
QLNRRYADNG SHRQQPHARR VVISADHEEE MHDLNLAATA GSPPSAV
//