ID Q63KS8_BURPS Unreviewed; 714 AA.
AC Q63KS8;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Family C39 unassigned peptidase {ECO:0000313|EMBL:CAH38754.1};
GN OrderedLocusNames=BPSS1285 {ECO:0000313|EMBL:CAH38754.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH38754.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH38754.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH38754.1,
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; BX571966; CAH38754.1; -; Genomic_DNA.
DR RefSeq; YP_111293.1; NC_006351.1.
DR AlphaFoldDB; Q63KS8; -.
DR STRING; 272560.BPSS1285; -.
DR MEROPS; C39.005; -.
DR KEGG; bps:BPSS1285; -.
DR PATRIC; fig|272560.6.peg.5485; -.
DR eggNOG; COG2274; Bacteria.
DR Proteomes; UP000000605; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd18567; ABC_6TM_CvaB_RaxB_like; 1.
DR CDD; cd03228; ABCC_MRP_Like; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF606; COLICIN V SECRETION-PROCESSING ATP-BINDING PROTEIN; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 170..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..140
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 172..433
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 488..714
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 714 AA; 78875 MW; 043683F786D2B86B CRC64;
MSSDSQAMWF NTNKVRPILQ DEVTECGLAC LAMIATWHGR DTTLRTLRNR YPVKIDSGLS
FFDLMEIAND LGMRARGLQF EANEIDALKL PCILHWGMNH YVVLTKVCYG SVHIVDPALG
ETKLPLAQAL TQITGYALEL NPDIGFKHVG TSDKIRLGDY LVGLTGIRKS ILLGVAGGIA
AQLLLLLGPS YVQLTIDEAL KKTDVDILYL LTILFGIVFL FDTLYANLVG NIKSYLRNIV
SQQLSANMVG HLARLPIGYY LFHNTGDSIS RVSSVSEIGR FLVDGLIGGL LNVFTCVITL
VLMLYYSPVL AGISLAGMVL FALSRLAIQP QLQDAMSQIL TRGAEADALL IENIRSAHSI
KLLSSETSRS SLWVNAFTQK LQAVRQQERL QLLFDAISKG IVHVEQLVIV TYGAWLVMHG
QSTIGIIYAF IQYKNLFADK FVDSIQLYVR RKVLQVHMDR VADVLQTETE EPAPDAPVRS
IEHFDGSLSI RALTYTPKGG RRAILEDVNL DVPAGAKIAI VGRTGSGKTT LLNLICGLYP
PAPGALFVGG VDLSEVNLRL YRKHVAAVTQ SDQLFRGTIR DNITNFAPAP RLGAMHEAAR
LACIERDIDV LDNRYDTPLG DTQKFLSAGQ MQRLLIARAL YCEPRLLILD EFSSNLDQAT
THEICRNVLT LPCTIVLVTH DASILSMVDR IYEMRDGRLA DITPARQPEL EVQK
//
