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Database: UniProt
Entry: Q63HW7_BURPS
LinkDB: Q63HW7_BURPS
Original site: Q63HW7_BURPS 
ID   Q63HW7_BURPS            Unreviewed;       296 AA.
AC   Q63HW7;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Exported protein {ECO:0000313|EMBL:CAH39788.1};
GN   OrderedLocusNames=BPSS2302 {ECO:0000313|EMBL:CAH39788.1};
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH39788.1, ECO:0000313|Proteomes:UP000000605};
RN   [1] {ECO:0000313|EMBL:CAH39788.1, ECO:0000313|Proteomes:UP000000605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243 {ECO:0000313|EMBL:CAH39788.1,
RC   ECO:0000313|Proteomes:UP000000605};
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA   Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA   Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA   Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA   Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA   Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA   Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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DR   EMBL; BX571966; CAH39788.1; -; Genomic_DNA.
DR   RefSeq; YP_112305.1; NC_006351.1.
DR   AlphaFoldDB; Q63HW7; -.
DR   STRING; 272560.BPSS2302; -.
DR   KEGG; bps:BPSS2302; -.
DR   PATRIC; fig|272560.6.peg.6753; -.
DR   eggNOG; COG0726; Bacteria.
DR   Proteomes; UP000000605; Chromosome 2.
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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..296
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004267203"
FT   DOMAIN          106..296
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   296 AA;  32520 MW;  D26E1604530F38F4 CRC64;
     MRHSGSRLTR FRLAAAACCL ALASAARPAF AGANAPAAAE PPTDAQRPAI LVYHRFSTSA
     PPDSMTVRVS TFGAQLAFLR AHGYTFVPLR DVVAWAASPS APLPDKAIAI TVDDGHRSVY
     ELLRPIVLRE RLPVTLFIYP SAISNASYAM TWDELRALRA TGRFDIESHT WWHPNFRTER
     RRLAPDAFRR FAATQFAHSR ARLEREIGGP VDLLAWPFGL YDDELTSLAA QAGYVAGFTL
     DARKVRRGDA PLALPRLLIV DSCTPAVLAR MLGERGDARA DSHADLHVDS HAEQSR
//
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