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LOLD_AQUAE
ID   LOLD_AQUAE              Reviewed;         224 AA.
AC   O66646;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=aq_297;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06596.1; -; Genomic_DNA.
DR   PIR; B70327; B70327.
DR   RefSeq; NP_213206.1; NC_000918.1.
DR   RefSeq; WP_010880144.1; NC_000918.1.
DR   PDB; 2PCJ; X-ray; 1.70 A; A/B=1-224.
DR   PDB; 2PCL; X-ray; 1.70 A; A=1-224.
DR   PDBsum; 2PCJ; -.
DR   PDBsum; 2PCL; -.
DR   AlphaFoldDB; O66646; -.
DR   SMR; O66646; -.
DR   STRING; 224324.aq_297; -.
DR   EnsemblBacteria; AAC06596; AAC06596; aq_297.
DR   KEGG; aae:aq_297; -.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_1_22_0; -.
DR   InParanoid; O66646; -.
DR   OMA; FVYQSHR; -.
DR   OrthoDB; 1181903at2; -.
DR   EvolutionaryTrace; O66646; -.
DR   Proteomes; UP000000798; 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: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; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR017911; MacB_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..224
FT                   /note="Lipoprotein-releasing system ATP-binding protein
FT                   LolD"
FT                   /id="PRO_0000092417"
FT   DOMAIN          5..224
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01708"
FT   STRAND          3..14
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   STRAND          17..28
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   HELIX           43..50
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   STRAND          57..63
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   HELIX           73..83
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   HELIX           99..109
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   HELIX           114..127
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   HELIX           143..154
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   STRAND          160..166
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   TURN            167..170
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   HELIX           173..188
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   STRAND          192..196
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   STRAND          206..213
FT                   /evidence="ECO:0007829|PDB:2PCJ"
FT   STRAND          216..222
FT                   /evidence="ECO:0007829|PDB:2PCJ"
SQ   SEQUENCE   224 AA;  24887 MW;  0804B347486A963C CRC64;
     MAEILRAENI KKVIRGYEIL KGISLSVKKG EFVSIIGASG SGKSTLLYIL GLLDAPTEGK
     VFLEGKEVDY TNEKELSLLR NRKLGFVFQF HYLIPELTAL ENVIVPMLKM GKPKKEAKER
     GEYLLSELGL GDKLSRKPYE LSGGEQQRVA IARALANEPI LLFADEPTGN LDSANTKRVM
     DIFLKINEGG TSIVMVTHER ELAELTHRTL EMKDGKVVGE ITRV
 
 
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