ID Q211Q3_RHOPB Unreviewed; 256 AA.
AC Q211Q3;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN OrderedLocusNames=RPC_3341 {ECO:0000313|EMBL:ABD88883.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD88883.1};
RN [1] {ECO:0000313|EMBL:ABD88883.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD88883.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) 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; CP000301; ABD88883.1; -; Genomic_DNA.
DR AlphaFoldDB; Q211Q3; -.
DR STRING; 316056.RPC_3341; -.
DR KEGG; rpc:RPC_3341; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_021264_8_0_5; -.
DR OrthoDB; 276604at2; -.
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; cd10917; CE4_NodB_like_6s_7s; 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 3: Inferred from homology;
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..256
FT /note="Chitooligosaccharide deacetylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004199694"
FT DOMAIN 60..244
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 256 AA; 27767 MW; F3AD6DFDBC82CCA7 CRC64;
MTASRLIAIA ALLAGVTPAQ AADCPRAGAL GTSRVLSVDA VTTPRVGLKS FPETLPLQDK
EVVLTFDDGP ANTTPQVLSA LSHECVQATF FMVGIGVAAL PKLVRRVAAE GHSIGTHTWS
HKNLKNLKPE EAAEEIDRGI AAVETALHGK ASRVPSTPFF RFPWFDSTPA LLDQLQSRGI
VVFGADLWAS DWNLMTPQQQ LTLVTGRLEA ARKGIILFHD PRAQTAAMLP DFLRYLRENH
YRVVHVVAKA EPNVTH
//
