ID Q1GJ85_RUEST Unreviewed; 1002 AA.
AC Q1GJ85;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN OrderedLocusNames=TM1040_0548 {ECO:0000313|EMBL:ABF63281.1};
OS Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=292414 {ECO:0000313|EMBL:ABF63281.1, ECO:0000313|Proteomes:UP000000636};
RN [1] {ECO:0000313|Proteomes:UP000000636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040 {ECO:0000313|Proteomes:UP000000636};
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 Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA Richardson P.;
RT "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABF63281.1, ECO:0000313|Proteomes:UP000000636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040 {ECO:0000313|EMBL:ABF63281.1,
RC ECO:0000313|Proteomes:UP000000636};
RX PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA Saunders E., Buchan A.;
RT "Ecological genomics of marine Roseobacters.";
RL Appl. Environ. Microbiol. 73:4559-4569(2007).
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 glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000256|ARBA:ARBA00010973}.
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DR EMBL; CP000377; ABF63281.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1GJ85; -.
DR STRING; 292414.TM1040_0548; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR KEGG; sit:TM1040_0548; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG1215; Bacteria.
DR eggNOG; COG3858; Bacteria.
DR HOGENOM; CLU_009182_0_0_5; -.
DR Proteomes; UP000000636; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10962; CE4_GT2-like; 1.
DR CDD; cd06423; CESA_like; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43630; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR PANTHER; PTHR43630:SF1; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000000636};
KW Transferase {ECO:0000313|EMBL:ABF63281.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 595..620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 880..903
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 368..557
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 1002 AA; 110422 MW; D9C002C8913CE03C CRC64;
MSLNESCNQL GVLVPDWLRL ETTPEGPVVK IESEESRAPL VDYRSTSGHA PDLMPVLEVD
TGSDKAGFLR NLSTPETAQS VTSQVLAQLR PLYAQGTCIS IPGLETADLD VLQPFFKTLT
SSLRSEGHSP CLILSGTSTA WQSRETTALF DKVILKLFLD PWVGTAPSPL ATDAWFEKTA
KAALQEIGKD KLVIALGTFA VEWVSGEPLP KVLPYAAAME KIAAAGAELR FSEKTSGSLA
SYRDPEGRLN KIWMQDVASL INQLVILQQL EIPNSAVWSL GLEDPGIWSV LQNRDLSHDA
LSADLALVKL DSYVSYRGEG ALLRLHRRQS PGIRQIGFDT ETGRVVSQSY DLLPRPYALE
RYGKPAGRKV VLTFDDGPHP VFSEQILDIL QETQTPATFF VTGKSVMNAP EVLNRMIDEG
HEIGAHTFSH PRMDQVSKTR ATLEYAMLDK VVAGAAGRQL TLYREPFQRS GGPVTADRVA
ALEIAWDRDM QVVGMDVVPH DWAGWSGREI ADFAIEEVER GAGNVILLHD GGEDRTASVE
ATRLIITELS AKGYEFTTVA DLTGSTRAAL MPVTEGGYQT FDRVSFSLVA WGQDAIVILF
WLALGIGVVR SVAILLLAVL NWRGHRTISL TTPKVAVIIP AHNEEKVIRS CIQSVRASDY
KNLEIIVVDD GSSDNTLNEI FAFSHMREVR LISQPNQGKW SALNRALMNT SAEIVVCIDA
DTQIEKSAIG HMVRHFDNPR IGAVAGKIIA GNKVNLLTRL QALEYTTAQN VERKAFDLIN
GMLVVPGALG AWRVAALRKA GHFSDETMTE DTDLTIEVNR AGYRIAYEPL ARGYTEVPER
IGQLLKQRLR WSFGMFQSAW KHKKAMFEGR SVGLISIPDM FIFGYLFPLL APIADLFVAI
LLYQMVSGGW DSGAVGAQNM QYLLAYLTLP ALEFVIAAFA LARDKDESMW SLLLFPVQRV
LYRPILYYSV IRAILRAITG RLFSWGAQKR LGRDYSLATS GT
//
