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LOLD_GLUOX
ID   LOLD_GLUOX              Reviewed;         231 AA.
AC   Q5FUV5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=GOX0077;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW59874.1; -; Genomic_DNA.
DR   RefSeq; WP_011251678.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FUV5; -.
DR   SMR; Q5FUV5; -.
DR   STRING; 290633.GOX0077; -.
DR   EnsemblBacteria; AAW59874; AAW59874; GOX0077.
DR   KEGG; gox:GOX0077; -.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_1_22_5; -.
DR   OMA; FVYQSHR; -.
DR   Proteomes; UP000006375; 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; 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..231
FT                   /note="Lipoprotein-releasing system ATP-binding protein
FT                   LolD"
FT                   /id="PRO_0000272091"
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   231 AA;  24841 MW;  933785BF8AD656E6 CRC64;
     MNEVSTGASA LRLEGLTRRF RSGEETLEIL SGAEFELRAG EIVALVAPSG TGKSTLLHLA
     GLLEAPSAGT VFVADRPASG LSDTVRTAIR RDQIGFVYQF HHLLGEFTAC ENVMLPQLIA
     GVSPRKARER ARDLLGRFGL SHRLDSLPGR LSGGEQQRTA IARALANQPK LLLADEPTGN
     LDIGTADHVF GELLRVVREE GAAALIATHN DELASRMDRT VTLRDGKLVP F
 
 
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