ID   NODB_SINFN              Reviewed;         215 AA.
AC   P50355;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Chitooligosaccharide deacetylase;
DE            EC=3.5.1.-;
DE   AltName: Full=Nodulation protein B;
GN   Name=nodB; OrderedLocusNames=NGR_a03420; ORFNames=y4hH;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7984092; DOI=10.1111/j.1365-2958.1994.tb00412.x;
RA   Relic B., Perret X., Estrada-Garcia M.T., Kopcinska J., Golinowski W.,
RA   Krishnan H.B., Pueppke S.G., Broughton W.J.;
RT   "Nod factors of Rhizobium are a key to the legume door.";
RL   Mol. Microbiol. 13:171-178(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000305}.
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DR   EMBL; X73362; CAA51773.1; -; Genomic_DNA.
DR   EMBL; U00090; AAB91696.1; -; Genomic_DNA.
DR   PIR; S34304; S34304.
DR   RefSeq; NP_443884.1; NC_000914.2.
DR   RefSeq; WP_010875356.1; NC_000914.2.
DR   AlphaFoldDB; P50355; -.
DR   SMR; P50355; -.
DR   STRING; 394.NGR_a03420; -.
DR   EnsemblBacteria; AAB91696; AAB91696; NGR_a03420.
DR   GeneID; 48977544; -.
DR   KEGG; rhi:NGR_a03420; -.
DR   PATRIC; fig|394.7.peg.351; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_021264_0_0_5; -.
DR   OMA; NHAMRDE; -.
DR   OrthoDB; 1701876at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   InterPro; IPR026402; Nodulat_NodB.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   TIGRFAMs; TIGR04243; nodulat_NodB; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nodulation; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..215
FT                   /note="Chitooligosaccharide deacetylase"
FT                   /id="PRO_0000172756"
FT   DOMAIN          18..209
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT   ACT_SITE        25
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        171
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   SITE            145
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        148..149
FT                   /note="RP -> S (in Ref. 1; CAA51773)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   215 AA;  23625 MW;  8A91E2B4E9D6D57F CRC64;
     MKQLDYLRTV PRSGTGAPSV YLTFDDGPNP VFTPEVLDVL AEHRVPATFF VIGAYAKDRP
     QLIRRMVAQG HEVANHTMTH PDLSACGRRD VERQVLEANR AIRMACPEAS VRHIRAPYGI
     WSDDVLTTSA NAGLAAVHWS VDPRDWSRPG IDAIVDAVLA SVRPGSIILL HDGCPPDELA
     NTDASFRDQT VAALSRLIPA LHDRGFIIRS LPQNH