ID   LOLD2_RHOPA             Reviewed;         232 AA.
AC   Q6N5P8;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Lipoprotein-releasing system ATP-binding protein LolD 2 {ECO:0000255|HAMAP-Rule:MF_01708};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01708};
GN   Name=lolD2 {ECO:0000255|HAMAP-Rule:MF_01708}; OrderedLocusNames=RPA2926;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(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; BX572602; CAE28367.1; -; Genomic_DNA.
DR   RefSeq; WP_011158475.1; NC_005296.1.
DR   AlphaFoldDB; Q6N5P8; -.
DR   SMR; Q6N5P8; -.
DR   STRING; 258594.RPA2926; -.
DR   PRIDE; Q6N5P8; -.
DR   EnsemblBacteria; CAE28367; CAE28367; RPA2926.
DR   GeneID; 66894009; -.
DR   KEGG; rpa:RPA2926; -.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_1_22_5; -.
DR   OMA; FVYQSHR; -.
DR   PhylomeDB; Q6N5P8; -.
DR   BioCyc; RPAL258594:TX73_RS14925-MON; -.
DR   Proteomes; UP000001426; 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..232
FT                   /note="Lipoprotein-releasing system ATP-binding protein
FT                   LolD 2"
FT                   /id="PRO_0000272137"
FT   DOMAIN          11..231
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
SQ   SEQUENCE   232 AA;  25382 MW;  7620AA997CD3EC4F CRC64;
     MEQGAEDIPV VYLHDIKRQY SQGEATLTIL DGAKLALWAG QSVALVAPSG SGKSTLLHIA
     GLLEHPDEGE VYVSGAATSA LTDAERTQIR RTDIGFVYQS HRLLPEFTAL ENVMLPQMIR
     GLKRKETISR SKEILSYLGL ADRITHRPSE LSGGEQQRVA IARAVANAPR VLFADEPTGN
     LDPHTADYVF NALMQLVKAT QVAMLIATHN MELAARMDRR VSLQDGVVVE LE