ID Q63QQ0_BURPS Unreviewed; 544 AA.
AC Q63QQ0;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Lipoprotein {ECO:0000313|EMBL:CAH36984.1};
GN OrderedLocusNames=BPSL2974 {ECO:0000313|EMBL:CAH36984.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH36984.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH36984.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH36984.1,
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; BX571965; CAH36984.1; -; Genomic_DNA.
DR RefSeq; WP_004194232.1; NZ_CP009538.1.
DR RefSeq; YP_109568.1; NC_006350.1.
DR AlphaFoldDB; Q63QQ0; -.
DR STRING; 272560.BPSL2974; -.
DR ESTHER; burma-q62gy2; Carboxypeptidase_S10.
DR GeneID; 56594223; -.
DR KEGG; bps:BPSL2974; -.
DR PATRIC; fig|272560.51.peg.2301; -.
DR eggNOG; COG2939; Bacteria.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR PANTHER; PTHR11802:SF472; SERINE CARBOXYPEPTIDASE CPVL-RELATED; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Lipoprotein {ECO:0000313|EMBL:CAH36984.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..544
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004266529"
FT REGION 29..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 57610 MW; 25064BB56C3B1DDF CRC64;
MPARKAQLLL AAVFSSLLIA ACNGDDAGSP ASAAASENSS GNIDASSGAD KPYRDPNRYS
SSGSASLSPS AVTENAAITH HQITVNGKTI NYTATAGHLS ARNPQSGAAE ASFFYVAYTA
DNQPLGKRPV TFFYNGGPGS STVWLHLGSF GPKRLVTGDP NANSPTPFPF VDNQETLLDT
TDLVFVDAIG TGFSEAIAPN TNQTFWGVDQ DAGAFRDFVI RYLQVNQRND SPKYLFGESY
GTPRTDVLAN LLETAGVKLD GIVLQSSILN YNSNCDMASN SVGGSNSGSS AVSCAGFVPS
YGAIGAYYQL DNPNPTNLPQ YADQMRLLTA GTYSPAVDAY LANHTPPSSS LVTTMSNATG
ATVPLWRANF NLLPTSYDNS YQLALIPGTL IGRYDARVNV PTNSPLASDG DPSSSFITKP
FTDTIGTYLP NVLKYTAKSA YAVQSNAIAS WDWSHDGLDL PDTIPDLAAA LTLNPALKVL
SLNGYHDIAT PFYQTELDLA RLGAQPNLTI KDYQGGHMVY LDDTSRPQEK ADLATFYAAA
PAAR
//
