LOLD1_RHOBA
ID LOLD1_RHOBA Reviewed; 229 AA.
AC Q7UX73;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Lipoprotein-releasing system ATP-binding protein LolD 1 {ECO:0000255|HAMAP-Rule:MF_01708};
DE EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01708};
GN Name=lolD1 {ECO:0000255|HAMAP-Rule:MF_01708}; OrderedLocusNames=RB1517;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(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; BX294135; CAD72136.1; -; Genomic_DNA.
DR RefSeq; NP_864457.1; NC_005027.1.
DR RefSeq; WP_011118407.1; NC_005027.1.
DR AlphaFoldDB; Q7UX73; -.
DR SMR; Q7UX73; -.
DR STRING; 243090.RB1517; -.
DR EnsemblBacteria; CAD72136; CAD72136; RB1517.
DR KEGG; rba:RB1517; -.
DR PATRIC; fig|243090.15.peg.709; -.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_1_22_0; -.
DR InParanoid; Q7UX73; -.
DR OMA; RMKDFDA; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0044874; P:lipoprotein localization to outer membrane; IBA:GO_Central.
DR GO; GO:0042953; P:lipoprotein transport; IEA:InterPro.
DR GO; GO:0089705; P:protein localization to outer membrane; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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..229
FT /note="Lipoprotein-releasing system ATP-binding protein
FT LolD 1"
FT /id="PRO_0000092454"
FT DOMAIN 2..229
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
SQ SEQUENCE 229 AA; 24463 MW; 0D2490C70E2F7500 CRC64;
MLVVSELSKS YPTAGEPLSV LRGVNLELSP GQSAAIVGPS GSGKTTLLQI LGTLDEPDSG
SVQINGQDPF ALDARERAAY RNQTIGFIFQ DHHLLPQLSV TENVLIPALA NGKPTSDDVS
RAAELIDAVG LSHRATHLPR ELSGGERERV AIARALLMQP SVVLADEPTG NLDSKTAKTI
TELLLRLQAE QNTVLVTVTH SLSLADEMNE RFELVDGALV RRGRFGITA