LOLD_CHRVO
ID LOLD_CHRVO Reviewed; 230 AA.
AC Q7NTU0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=CV_2963;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(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; AE016825; AAQ60631.1; -; Genomic_DNA.
DR RefSeq; WP_011136510.1; NC_005085.1.
DR AlphaFoldDB; Q7NTU0; -.
DR SMR; Q7NTU0; -.
DR STRING; 243365.CV_2963; -.
DR EnsemblBacteria; AAQ60631; AAQ60631; CV_2963.
DR GeneID; 66368663; -.
DR KEGG; cvi:CV_2963; -.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_1_22_4; -.
DR OMA; HDMSLAR; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000001424; 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..230
FT /note="Lipoprotein-releasing system ATP-binding protein
FT LolD"
FT /id="PRO_0000092432"
FT DOMAIN 5..230
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
SQ SEQUENCE 230 AA; 24912 MW; 7AC4AA7D74927F43 CRC64;
MNKVLSCRSL GKRYQEGKLA LDVLSGVDLE VGKGEHLAIV GASGSGKSTL LHLLGGLDTP
TAGTVEVLGR DLSKLSETER GKLRNESMGF VYQFHHLLPE FTALENVMMP LLIRRMDKGE
AARRAAEMLE RVGLGKRLEH KPGELSGGER QRAAIARALV TQPACLLADE PTGNLDAHTA
SQVFELMLEL NRTLGTSLII VTHDLELAGR TQRVLRLNEG RLAVSDTVSA
