ID   A0A257KPT4_9BRAD        Unreviewed;       351 AA.
AC   A0A257KPT4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=CFE29_15315 {ECO:0000313|EMBL:OYU89373.1};
OS   Bradyrhizobiaceae bacterium PARB1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae.
OX   NCBI_TaxID=2015576 {ECO:0000313|EMBL:OYU89373.1, ECO:0000313|Proteomes:UP000216768};
RN   [1] {ECO:0000313|EMBL:OYU89373.1, ECO:0000313|Proteomes:UP000216768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PARB1 {ECO:0000313|EMBL:OYU89373.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Is involved in generating a small heat-stable compound (Nod),
CC       an acylated oligomer of N-acetylglucosamine, that stimulates mitosis in
CC       various plant protoplasts. {ECO:0000256|ARBA:ARBA00003236}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:OYU89373.1}.
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; NKIY01000004; OYU89373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257KPT4; -.
DR   Proteomes; UP000216768; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd10968; CE4_Mlr8448_like_5s; 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; PTHR34216; -; 1.
DR   PANTHER; PTHR34216:SF7; 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   Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          91..280
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|Pfam:PF01522"
SQ   SEQUENCE   351 AA;  38943 MW;  84CE2DE4E256352D CRC64;
     MKQIRNTIIR AGLDALYFSG AHRVLRPFFG GVGTIFMLHN VRPAHTGLFQ PNRHLEITPD
     FLRATLAYLR ATGVDIVTPD EMHRRLREQD FSRRFACFTC DDGYRDNRDH MLPAMRDFDA
     PFSVFVTSDF ASGTGRLWWV ALERVVAKAE RLEAPIDGNM IQLATATLPE KEMGFDRLHG
     WLRSLGEADL RREMTALCQQ AGIDEEAICR ELCLSWDELK PFAADPLLTI GAHTLTHCNL
     AKQTEAVAAH ELTASRTNIE NALQKPALHL AYPYGDRAAA GSREFALAQA AGFQTAVTTR
     PGVIAAENAT QLTALPRVSL NGNYQDTRYL PVLTSGAATA MWNGFQRVGQ G
//