ID A7IEY0_XANP2 Unreviewed; 360 AA.
AC A7IEY0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN OrderedLocusNames=Xaut_1324 {ECO:0000313|EMBL:ABS66573.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS66573.1, ECO:0000313|Proteomes:UP000002417};
RN [1] {ECO:0000313|EMBL:ABS66573.1, ECO:0000313|Proteomes:UP000002417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) 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}.
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DR EMBL; CP000781; ABS66573.1; -; Genomic_DNA.
DR AlphaFoldDB; A7IEY0; -.
DR STRING; 78245.Xaut_1324; -.
DR KEGG; xau:Xaut_1324; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_062195_0_0_5; -.
DR OrthoDB; 9784220at2; -.
DR PhylomeDB; A7IEY0; -.
DR Proteomes; UP000002417; Chromosome.
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 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; GLYCOSYL TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR10587:SF134; LIPOPROTEIN-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Reference proteome {ECO:0000313|Proteomes:UP000002417}.
FT DOMAIN 117..318
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 360 AA; 38263 MW; 407E8F1CC9ADDE8F CRC64;
MFPRATARDR PALAKGRAGA YAKDRSFAPV EFAVSVRSTL CLALLLLPAS FPVLAGPAAG
PACYSPAALA AKPGEEIVRP RAGGPVTLPD MATPTLPPVP AALRGSIRRV ELPPGEKLVA
LTFDLCEASA EISGYDGALV DYLRAENVAA TFFAGGKWLM SHTERGDQLT ADHQFEMGNH
TWSHANLTVR TGDAMRRQVD DADVALALRR TEVKAKGCML PSAPAQATGG AELFRFPYGS
CSAESLNYVN DTGHLAIQWD VDSGDPAFIG AKGMAEDMLR SIRPGSIVLM HANGRGKHTA
EALRILIPAL RAKGYRFATV SQLLAAGRPV IADTCYSLKP GDTRVYDDAA RTGKRILPVQ
//
