ID   A0A117S378_9FIRM        Unreviewed;       384 AA.
AC   A0A117S378;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=NodB homology domain-containing protein {ECO:0000259|Pfam:PF01522};
GN   ORFNames=APF76_17945 {ECO:0000313|EMBL:KUO48768.1};
OS   Desulfitibacter sp. BRH_c19.
OC   Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC   Desulfitibacter.
OX   NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO48768.1, ECO:0000313|Proteomes:UP000053015};
RN   [1] {ECO:0000313|EMBL:KUO48768.1, ECO:0000313|Proteomes:UP000053015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO48768.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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:KUO48768.1}.
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; LOER01000047; KUO48768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117S378; -.
DR   STRING; 1734395.APF76_17945; -.
DR   Proteomes; UP000053015; 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; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR34216; -; 1.
DR   PANTHER; PTHR34216:SF3; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          158..282
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|Pfam:PF01522"
FT   REGION          70..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  43878 MW;  8362E9BDB5791B25 CRC64;
     MNNFPGGKRR NYRLIGEFLV RKRLLGVRIL TARYSMIVIV TLLFLFTFGC GVSDADQKVQ
     DNTSEEIINQ DEKENEEKSQ ENSGNNIEEL QEGPLPANEA GQVMVLMYHR FGDTESTWQR
     TWGNFRVDIE RLYEEGYRLI SIKDYLNNTI DIPAGYSPVI LTFDDGYSNQ FSVEKIEDEW
     VLKPQTAAGI MFEFYQEHPD FGLEGIFYVN SQPFNGGNWR IAAEYLVGEL GMDIGNHTRT
     HINMNEHGPN KVIEELGGLV KDFQEVLPNY QIDSLALPFG VAPSSPETLS GEYDGVKYEN
     KGVLLVGANP ALSPIAEKYN PLKIPRIRGD EENFTKWLDY FIENPHLRYV SDGDPEKITV
     PSDMNDILSP EVLEDKRLQV YHRE
//