LOLD_LEGPA
ID LOLD_LEGPA Reviewed; 227 AA.
AC Q5X2Z8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=lpp2238;
OS Legionella pneumophila (strain Paris).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Paris;
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(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}.
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DR EMBL; CR628336; CAH13390.1; -; Genomic_DNA.
DR RefSeq; WP_015961404.1; NC_006368.1.
DR AlphaFoldDB; Q5X2Z8; -.
DR SMR; Q5X2Z8; -.
DR KEGG; lpp:lpp2238; -.
DR LegioList; lpp2238; -.
DR HOGENOM; CLU_000604_1_22_6; -.
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..227
FT /note="Lipoprotein-releasing system ATP-binding protein
FT LolD"
FT /id="PRO_0000272100"
FT DOMAIN 6..227
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 227 AA; 25187 MW; 801248ECE4D6FA78 CRC64;
MNDIILTSQK LYKSYHDGTS RVEVLKGVDL AITKGDRIAI IGPSGSGKST LLHLLGGLDK
PTSGLITLGK VDWQKINEKQ RCQLRNQQLG FVYQFHHLLP EFTALENVMM PLLLAGMAVK
DAEEKAINML EQVGLKPRLA HKPAQLSGGE RQRVAIARAL VHQPHCVLAD EPTGNLDEAT
ASKVFDLMLE LNKKMNTALV IVTHDQRIAE RMDRVLVLHE GSLYARE
