LOLD_ZYMMA
ID LOLD_ZYMMA Reviewed; 232 AA.
AC F8DT93; P74997; Q5NQC3;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=Zmob_0989;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 /
OS NCIMB 8938 / NRRL B-806 / ZM1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=555217;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10988 / DSM 424 / CCUG 17860 / LMG 404 / NCIMB 8938 / NRRL
RC B-806 / ZM1;
RX PubMed=8661924; DOI=10.1007/s002030050334;
RA Peekhaus N., Kramer R.;
RT "The gluEMP operon from Zymomonas mobilis encodes a high-affinity glutamate
RT carrier with similarity to binding-protein-dependent transport systems.";
RL Arch. Microbiol. 165:325-332(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10988 / DSM 424 / CCUG 17860 / LMG 404 / NCIMB 8938 / NRRL
RC B-806 / ZM1;
RX PubMed=21725006; DOI=10.1128/jb.05395-11;
RA Pappas K.M., Kouvelis V.N., Saunders E., Brettin T.S., Bruce D., Detter C.,
RA Balakireva M., Han C.S., Savvakis G., Kyrpides N.C., Typas M.A.;
RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. mobilis
RT lectotype strain ATCC 10988.";
RL J. Bacteriol. 193:5051-5052(2011).
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; X84019; CAA58842.1; -; Genomic_DNA.
DR EMBL; CP002850; AEH62824.1; -; Genomic_DNA.
DR PIR; S71374; S71374.
DR RefSeq; WP_014500819.1; NC_017262.1.
DR AlphaFoldDB; F8DT93; -.
DR SMR; F8DT93; -.
DR STRING; 555217.Zmob_0989; -.
DR EnsemblBacteria; AEH62824; AEH62824; Zmob_0989.
DR KEGG; zmm:Zmob_0989; -.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_1_22_5; -.
DR OMA; FVYQSHR; -.
DR Proteomes; UP000001494; 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; Translocase; Transport.
FT CHAIN 1..232
FT /note="Lipoprotein-releasing system ATP-binding protein
FT LolD"
FT /id="PRO_0000414231"
FT DOMAIN 11..232
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"
FT CONFLICT 25
FT /note="H -> D (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="R -> H (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="Q -> R (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="G -> S (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="H -> Y (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="D -> H (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="S -> P (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="E -> Q (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="G -> S (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="R -> G (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="A -> T (in Ref. 1; CAA58842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 25835 MW; 2783591847A31712 CRC64;
MNSPLSYNNV IEVTDLQRAF KQGEHEIQIL RGIDLIVRRG EILALLGPSG AGKSTFLQAI
GLLENGFTGS INILGQEIGS LNDKERTAIR RDHLGFVYQF HHLLPDFSAL ENVMLPQLIQ
GKSSHQAKEH AHFLLNSLKL EERLKHYPSQ LSGGEQQRVA VARALANRPA LVLADEPTGN
LDEATGDIVL HEFLRLVRRQ GSAAIIATHN MAMARKMDRI VTLHDGRLIE EY
