ID   G7Z6W4_AZOL4            Unreviewed;       350 AA.
AC   G7Z6W4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   OrderedLocusNames=AZOLI_2987 {ECO:0000313|EMBL:CBS88157.1};
OS   Azospirillum lipoferum (strain 4B).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS88157.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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DR   EMBL; FQ311868; CBS88157.1; -; Genomic_DNA.
DR   RefSeq; WP_014249131.1; NC_016622.1.
DR   AlphaFoldDB; G7Z6W4; -.
DR   STRING; 862719.AZOLI_2987; -.
DR   KEGG; ali:AZOLI_2987; -.
DR   HOGENOM; CLU_030024_0_1_5; -.
DR   OrthoDB; 9782872at2; -.
DR   Proteomes; UP000005667; Chromosome.
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; cd10973; CE4_DAC_u4_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: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.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..350
FT                   /note="Chitooligosaccharide deacetylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003506655"
FT   DOMAIN          96..350
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   350 AA;  38148 MW;  F3C99260D566F4F3 CRC64;
     MPFRRAVRVF AAAALSFWTA LVPALRPAVA DSAPPPGASA VVFAYDRFGE DQNPSISIRI
     DQFEAHLDEL TDGDYRVLPL PKILEALRTG KPLPDRTVAI TIDEASRSAF TEAWPRLKAA
     NLPFTLFVAT DAVDRGSPTH MTWGEIRQLA AAGVTIGALG TSTQSMLARS PEHLAADLRR
     MSDRFQAELG RRPTIFSYPQ GEYSLAVRQL VMDQGFAAAF GQQSGVLHAQ ADPWSLPRFV
     MNETYGNVDR FELAANALPL PVSDLTPDDP LVTVNPPPLG FTIADGVGDS SKLACFATGQ
     GRTALERIAE DRVEVRIKDP FPPGRARVNC TLPTADGRWR WLGVQFLIPE
//