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Database: UniProt
Entry: J7IUF4_DESMD
LinkDB: J7IUF4_DESMD
Original site: J7IUF4_DESMD 
ID   J7IUF4_DESMD            Unreviewed;       251 AA.
AC   J7IUF4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   OrderedLocusNames=Desmer_3661 {ECO:0000313|EMBL:AFQ45497.1};
OS   Desulfosporosinus meridiei (strain ATCC BAA-275 / DSM 13257 / KCTC 12902 /
OS   NCIMB 13706 / S10).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=768704 {ECO:0000313|EMBL:AFQ45497.1, ECO:0000313|Proteomes:UP000005262};
RN   [1] {ECO:0000313|EMBL:AFQ45497.1, ECO:0000313|Proteomes:UP000005262}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC   {ECO:0000313|Proteomes:UP000005262};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
RN   [2] {ECO:0000313|Proteomes:UP000005262}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC   {ECO:0000313|Proteomes:UP000005262};
RA   Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Tapia R., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Peters L., Pitluck S., Woyke T., Pester M., Spring S., Ollivier B.,
RA   Rattei T., Klenk H.-P., Wagner M., Loy A.;
RT   "Finished genome of Desulfosporosinus meridiei DSM 13257.";
RL   Submitted (AUG-2012) 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; CP003629; AFQ45497.1; -; Genomic_DNA.
DR   RefSeq; WP_014904406.1; NC_018515.1.
DR   AlphaFoldDB; J7IUF4; -.
DR   STRING; 768704.Desmer_3661; -.
DR   KEGG; dmi:Desmer_3661; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_021264_0_2_9; -.
DR   OrthoDB; 61520at2; -.
DR   Proteomes; UP000005262; 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:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd10950; CE4_BsYlxY_like; 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   Carbohydrate metabolism {ECO:0000313|EMBL:AFQ45497.1};
KW   Glycosidase {ECO:0000313|EMBL:AFQ45497.1};
KW   Hydrolase {ECO:0000313|EMBL:AFQ45497.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000313|EMBL:AFQ45497.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Xylan degradation {ECO:0000313|EMBL:AFQ45497.1}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          50..235
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   251 AA;  28060 MW;  1BE35FB9D533F763 CRC64;
     MFINLKISRR ILSFGGIFFL LIVGIVAGRW VVASNTPVPK PIDQITTDQK LMALTINVDW
     GEEFIPAILD ELEKNKAQVT FFVTGRWAKK NPDLLKEIYN RGHQIENHGY SHPHPDQLSV
     GANQEEIKKT ESIVEGIIGK KTQLYAPPYG EKGASGLRAA HEMGYRTILW TLDTVDWRPD
     STPEIIAKRI VNPAIKFGIK PNKSGAIVLM HPKANTVKAL PVILEQLAKE GYIFQTLDEL
     ITYDQSGDTT S
//
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