LOLD_SACD2
ID LOLD_SACD2 Reviewed; 228 AA.
AC Q21JQ9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Sde_1810;
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD81070.1; -; Genomic_DNA.
DR RefSeq; WP_011468290.1; NC_007912.1.
DR AlphaFoldDB; Q21JQ9; -.
DR SMR; Q21JQ9; -.
DR STRING; 203122.Sde_1810; -.
DR EnsemblBacteria; ABD81070; ABD81070; Sde_1810.
DR KEGG; sde:Sde_1810; -.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; PRREEVM; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000001947; Chromosome.
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; Reference proteome; Translocase; Transport.
FT CHAIN 1..228
FT /note="Lipoprotein-releasing system ATP-binding protein
FT LolD"
FT /id="PRO_0000272145"
FT DOMAIN 6..228
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 228 AA; 24775 MW; 223CEB232493AE87 CRC64;
MSTPVIKCLN VVKGYSEGPQ KVEVLRGVNL QIEQGQHIAI VGASGSGKST LLNVLGGLDK
PDAGEVWVNE KAFSSLNDNK RGLVRNQELG FVYQFHHLLP EFTALENVMM PCLIAGVKKA
QAKQKAEALL DKVGLSHRLD HKPAELSGGE RQRVAIARAL VNEPACVLMD EPTGNLDTEN
AESIQSLMKE LSAQLQTSFI VVTHDLVLAN TMNQVYRLEA GVLNKQGQ