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Database: UniProt
Entry: A0A0U5MEL2_9PROT
LinkDB: A0A0U5MEL2_9PROT
Original site: A0A0U5MEL2_9PROT 
ID   A0A0U5MEL2_9PROT        Unreviewed;       278 AA.
AC   A0A0U5MEL2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=XM1_0894 {ECO:0000313|EMBL:CUW37963.1};
OS   Magnetospirillum sp. XM-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW37963.1, ECO:0000313|Proteomes:UP000063191};
RN   [1] {ECO:0000313|Proteomes:UP000063191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wang Y.;
RL   Submitted (DEC-2015) 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   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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DR   EMBL; LN997848; CUW37963.1; -; Genomic_DNA.
DR   RefSeq; WP_068430159.1; NZ_LN997848.1.
DR   AlphaFoldDB; A0A0U5MEL2; -.
DR   STRING; 1663591.XM1_0894; -.
DR   KEGG; magx:XM1_0894; -.
DR   PATRIC; fig|1663591.3.peg.892; -.
DR   OrthoDB; 9814639at2; -.
DR   Proteomes; UP000063191; Chromosome I.
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; cd10918; CE4_NodB_like_5s_6s; 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:SF8; POLYSACCHARIDE DEACETYLASE-LIKE PROTEIN; 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}.
FT   DOMAIN          78..278
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   278 AA;  29273 MW;  271B9814A47F3BA2 CRC64;
     MSLRTLAAPL ALAAWRATGP LRANPPGAVR ILILHDVPEA QFAALADLIA VLQRSAGLIT
     PGQAEARLAG GAPADGKAPV LLSFDDGFRS NFRLTREILD PLGVKALFFV CPALVDMAPE
     DRRAAIGANI FRGRRGADGL DLMDWEQLKG LAASGHEIGC HSARHVSLVG LEAGELEDEV
     GIAKTRMAAV LGQTSPWFAF PFGDVANIDR TALGIIGRHF PLCRSGVRGL AHAGSHPLAL
     PAESVDLGAP PALRLLAAEG GMAPLYRGRL RRLEEMAS
//
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