ID Q6MI90_BDEBA Unreviewed; 383 AA.
AC Q6MI90;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Putative polysaccharide deacetylase {ECO:0000313|EMBL:CAE78090.1};
DE EC=3.5.1.- {ECO:0000313|EMBL:CAE78090.1};
GN OrderedLocusNames=Bd3279 {ECO:0000313|EMBL:CAE78090.1};
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE78090.1, ECO:0000313|Proteomes:UP000008080};
RN [1] {ECO:0000313|EMBL:CAE78090.1, ECO:0000313|Proteomes:UP000008080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC {ECO:0000313|Proteomes:UP000008080};
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
RN [2] {ECO:0007829|PDB:5JP6}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=27211869; DOI=10.1038/srep26010;
RA Lambert C., Lerner T.R., Bui N.K., Somers H., Aizawa S., Liddell S.,
RA Clark A., Vollmer W., Lovering A.L., Sockett R.E.;
RT "Interrupting peptidoglycan deacetylation during Bdellovibrio predator-prey
RT interaction prevents ultimate destruction of prey wall, liberating
RT bacterial-ghosts.";
RL Sci. Rep. 6:26010-26010(2016).
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DR EMBL; BX842655; CAE78090.1; -; Genomic_DNA.
DR PDB; 5JP6; X-ray; 1.50 A; A=1-383.
DR PDBsum; 5JP6; -.
DR AlphaFoldDB; Q6MI90; -.
DR SMR; Q6MI90; -.
DR STRING; 264462.Bd3279; -.
DR KEGG; bba:Bd3279; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_728944_0_0_7; -.
DR Proteomes; UP000008080; 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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5JP6};
KW Hydrolase {ECO:0000313|EMBL:CAE78090.1};
KW Metal-binding {ECO:0007829|PDB:5JP6};
KW Reference proteome {ECO:0000313|Proteomes:UP000008080};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0007829|PDB:5JP6}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..383
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004276556"
FT DOMAIN 169..360
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:5JP6"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:5JP6"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:5JP6"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:5JP6"
FT DISULFID 79..109
FT /evidence="ECO:0007829|PDB:5JP6"
SQ SEQUENCE 383 AA; 42819 MW; 7A1A4EF645C565BC CRC64;
MYMKKLVFGG MLIVSAASLV GCGSQIGSSV RQAVSDNQSA QTLVEWENSE ANPEALFANW
RHEFMVDSSK RESMKTELCK ELQALPAQDL TLFENEIRDE NNRALVSGCK EELLAQVDEH
FDEQRESMSV PGHALKAVQS RNSFRFPDNT QKRDMSNGYM AVRGDVARKE VVLTFDDGPH
GLYTDAILRA LKEVNAKAMF FATGKSVRTN PEALKRVAAD GHVIGSHSIT HACLGTSVAC
YKQMGNRNLT FDEAAAEVRG GHQAVFDVLG WVDPVFRFPY GETSKDLKAF LKTKSTGEFA
WNIESDDWRT QSNEQLLARV LANVESQGRG IVLFHDIQRR TAEIMPQFLR ELYNRGYSVV
LLTAADPSAK YNSKLVKRKQ QLP
//
