ID   LOLD_BURPS              Reviewed;         249 AA.
AC   Q63SP4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Lipoprotein-releasing system ATP-binding protein LolD {ECO:0000255|HAMAP-Rule:MF_01708};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01708};
GN   Name=lolD {ECO:0000255|HAMAP-Rule:MF_01708}; OrderedLocusNames=BPSL2276;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., 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   -!- FUNCTION: Part of the ABC transporter complex LolCDE involved in the
CC       translocation of mature outer membrane-directed lipoproteins, from the
CC       inner membrane to the periplasmic chaperone, LolA. Responsible for the
CC       formation of the LolA-lipoprotein complex in an ATP-dependent manner.
CC       {ECO:0000255|HAMAP-Rule:MF_01708}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (LolD) and
CC       two transmembrane proteins (LolC and LolE). {ECO:0000255|HAMAP-
CC       Rule:MF_01708}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01708}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01708}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Lipoprotein
CC       translocase (TC 3.A.1.125) family. {ECO:0000255|HAMAP-Rule:MF_01708}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH36279.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX571965; CAH36279.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004195923.1; NZ_CP009538.1.
DR   RefSeq; YP_108872.1; NC_006350.1.
DR   AlphaFoldDB; Q63SP4; -.
DR   SMR; Q63SP4; -.
DR   STRING; 272560.BPSL2276; -.
DR   EnsemblBacteria; CAH36279; CAH36279; BPSL2276.
DR   GeneID; 56596070; -.
DR   KEGG; bps:BPSL2276; -.
DR   PATRIC; fig|272560.6.peg.2585; -.
DR   eggNOG; COG1136; Bacteria.
DR   OMA; VHARGMT; -.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0044873; P:lipoprotein localization to membrane; IEA:InterPro.
DR   GO; GO:0042953; P:lipoprotein transport; IEA:InterPro.
DR   CDD; cd03255; ABC_MJ0796_LolCDE_FtsE; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015854; ABC_transpr_LolD.
DR   InterPro; IPR011924; LolD_lipo_ATP-bd.
DR   InterPro; IPR017911; MacB_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24220:SF654; PTHR24220:SF654; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02211; LolD_lipo_ex; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51244; LOLD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..249
FT                   /note="Lipoprotein-releasing system ATP-binding protein
FT                   LolD"
FT                   /id="PRO_0000272065"
FT   DOMAIN          24..249
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
SQ   SEQUENCE   249 AA;  27407 MW;  17A2181E077DD35A CRC64;
     MNDRVFEQTM NQNHQDGGAR ECVLEARGVT KTFVQGGFNV QVLDNAQVSV RRGEKLAIVG
     ASGSGKSTLL HVLGGLDEPS AGQVSLLGKP FTQLAERERN ELRNRALGFV YQFHHLLPEF
     TALDNVAMPL RIRRMSTEEA RRHAREMLEQ VGLGARAKHR PGELSGGERQ RVAIARALVT
     KPACVLADEP TGNLDGSTAD HVFHLMLELS RTLDTSFVIV THDPDLAARC DRILRLRDGV
     LHEEPAVPV