ID   LOLD_FRATH              Reviewed;         231 AA.
AC   Q2A4V5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=FTL_0475;
OS   Francisella tularensis subsp. holarctica (strain LVS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=376619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVS;
RA   Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA   Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA   Garcia E.;
RT   "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT   Strain).";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AM233362; CAJ78915.1; -; Genomic_DNA.
DR   RefSeq; WP_003017997.1; NZ_CP009694.1.
DR   AlphaFoldDB; Q2A4V5; -.
DR   SMR; Q2A4V5; -.
DR   GeneID; 60807288; -.
DR   KEGG; ftl:FTL_0475; -.
DR   OMA; HDMSLAR; -.
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; Translocase; Transport.
FT   CHAIN           1..231
FT                   /note="Lipoprotein-releasing system ATP-binding protein
FT                   LolD"
FT                   /id="PRO_0000272085"
FT   DOMAIN          6..230
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
SQ   SEQUENCE   231 AA;  25727 MW;  63E0114C27A1B61B CRC64;
     MNDVVLSCKN VSKKYTEFKT DIAILKDVNL EIKKGEKVAI LGLSGSGKTT LLNVLGGLDK
     CSAGEVYLMG ERFDNQSVNK RAKMRNKHLG FIYQLHHLLP EFTAIENVMI PLAITKKYTK
     KESIKLANEI LKKVGLDHRA DHKPAELSGG ERQRVAIARA LVTNPNCILA DEPTGNLDSQ
     RSESIFALMQ QLSDDFGTSF VIVTHDEKLA SRMNKIYRLV DGELELVINS N