ID   LOLD_PORGI              Reviewed;         219 AA.
AC   Q7MU65;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=PG_1692;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ66706.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7MU65; -.
DR   SMR; Q7MU65; -.
DR   STRING; 242619.PG_1692; -.
DR   EnsemblBacteria; AAQ66706; AAQ66706; PG_1692.
DR   KEGG; pgi:PG_1692; -.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_1_22_10; -.
DR   OMA; LPWLTCF; -.
DR   Proteomes; UP000000588; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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   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..219
FT                   /note="Lipoprotein-releasing system ATP-binding protein
FT                   LolD"
FT                   /id="PRO_0000092447"
FT   DOMAIN          3..219
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
SQ   SEQUENCE   219 AA;  24188 MW;  9E23E7AE1802ED1B CRC64;
     MIIEARNIRK SFGSLEVLKG VDIAIDRGEI VSIVGTSGAG KTTLLQILGT LDRADSGELR
     IDGTDIMGMN NRKQAEFRNR RLGFIFQFHR LLPEFTALEN VMIPALIAGK SRKEASCEAE
     RLLSDLNLSD RASHKPSELS GGEKQRIAVA RALVNHPAII LADEPSGSLD SAHKEELHAL
     FFRLCREMGQ TFLIVTHDEK LAAGTDRILH MRDGLLFSE