LOLD_TREPA
ID LOLD_TREPA Reviewed; 226 AA.
AC O83590;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=TP_0581;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC65555.1; -; Genomic_DNA.
DR PIR; C71307; C71307.
DR RefSeq; WP_010882027.1; NC_021490.2.
DR AlphaFoldDB; O83590; -.
DR SMR; O83590; -.
DR STRING; 243276.TPANIC_0581; -.
DR EnsemblBacteria; AAC65555; AAC65555; TP_0581.
DR GeneID; 57879104; -.
DR KEGG; tpa:TP_0581; -.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_1_22_12; -.
DR OMA; GRMPRWR; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000000811; 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; 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; 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..226
FT /note="Lipoprotein-releasing system ATP-binding protein
FT LolD"
FT /id="PRO_0000092462"
FT DOMAIN 6..226
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 226 AA; 25299 MW; 2EBA1B962BEF70E3 CRC64;
MNDPILSVEQ VSKSFCCATE RIQILSDVSF SVPRAVKVAI TGESGCGKST LLNIIGGMEH
ADSGIVRVLS CDVLTLHEHA LTEYRRQFLG LVFQFHHLLR DFTALENVML PGLIAGKSYR
EVRARAYELL EKVRVVQRAH HFPAQMSGGE RQRTAVARAL INDPTLILAD EPTGNLDPKN
ALIVQDLLFS LTEEYQKTLL IVTHDPRIAS MTDYRYQLQQ GSLIRI