ID G8PKT9_PSEUV Unreviewed; 330 AA.
AC G8PKT9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN OrderedLocusNames=PSE_3557 {ECO:0000313|EMBL:AEV38061.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV38061.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV38061.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV38061.1,
RC ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
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; CP003147; AEV38061.1; -; Genomic_DNA.
DR AlphaFoldDB; G8PKT9; -.
DR STRING; 911045.PSE_3557; -.
DR KEGG; psf:PSE_3557; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_030024_1_2_5; -.
DR Proteomes; UP000005634; Chromosome.
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; cd10968; CE4_Mlr8448_like_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:SF7; 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 Hydrolase {ECO:0000313|EMBL:AEV38061.1};
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 68..330
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 330 AA; 37351 MW; 8B19DDD35B3E6829 CRC64;
MTAGDGVIFT LHRVLPASDR AFQPNKLLEV TPKFLRDTVK QVRASGYEFV SLDVALERLR
AGEKFACRFA VLTFDDGYKD NRDVAYPILK ELGVPFTIFI SSEYSNHNSE LWWIILEQLI
AENTSVSLRY GERQFNYDCS SLELKEAAFE ASRCMLISEV PETAQRDVVR EAAERYGHDW
RALCQELILS FEELKELAQD PLVSLGAHTD THPMLARLST EEEIRQHIQA GQEEMVARLG
TRPTMLAYPY GFAEAVDRRC EAVAEELGFA AAVTTQPGTL SAKNLERLYH LPRVSLNGLH
QNQRMVDVYL TGAAFAAYHA VKRVRSLLQM
//
