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LPTD_ALIF1
ID   LPTD_ALIF1              Reviewed;         786 AA.
AC   Q5E862;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=LPS-assembly protein LptD {ECO:0000255|HAMAP-Rule:MF_01411};
DE   Flags: Precursor;
GN   Name=lptD {ECO:0000255|HAMAP-Rule:MF_01411}; Synonyms=imp, ostA;
GN   OrderedLocusNames=VF_0289;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC   -!- FUNCTION: Together with LptE, is involved in the assembly of
CC       lipopolysaccharide (LPS) at the surface of the outer membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01411}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC       complex. Interacts with LptE and LptA. {ECO:0000255|HAMAP-
CC       Rule:MF_01411}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01411}.
CC   -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01411}.
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DR   EMBL; CP000020; AAW84784.1; -; Genomic_DNA.
DR   RefSeq; WP_011261100.1; NC_006840.2.
DR   RefSeq; YP_203672.1; NC_006840.2.
DR   AlphaFoldDB; Q5E862; -.
DR   SMR; Q5E862; -.
DR   STRING; 312309.VF_0289; -.
DR   PRIDE; Q5E862; -.
DR   EnsemblBacteria; AAW84784; AAW84784; VF_0289.
DR   KEGG; vfi:VF_0289; -.
DR   PATRIC; fig|312309.11.peg.283; -.
DR   eggNOG; COG1452; Bacteria.
DR   HOGENOM; CLU_009039_0_0_6; -.
DR   OMA; DYSHLDW; -.
DR   OrthoDB; 100018at2; -.
DR   Proteomes; UP000000537; Chromosome I.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0015920; P:lipopolysaccharide transport; IEA:InterPro.
DR   GO; GO:0010033; P:response to organic substance; IEA:InterPro.
DR   HAMAP; MF_01411; LPS_assembly_LptD; 1.
DR   InterPro; IPR020889; LipoPS_assembly_LptD.
DR   InterPro; IPR007543; LptD_C.
DR   InterPro; IPR005653; OstA-like_N.
DR   Pfam; PF04453; LptD; 1.
DR   Pfam; PF03968; LptD_N; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           25..786
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_0000020292"
SQ   SEQUENCE   786 AA;  89296 MW;  D9DE906B5A9207C2 CRC64;
     MSFTSRSLLA SFTGCLLYGT PAIADNGSEP VSPENGIVFP LQTDAVNSCE VPDKKSKEEE
     DQQPVLIQAD SVEASNNSKA VYKGNVHIIK GRQEIKADSI TLHQQENIAI AEGNVDYSSM
     EMRTTSDKVT TNLSTEDTTM VNTAYKMSCQ PIRGQAGRVL KTGQEIYQLE DASFTTCPAD
     DNSWRFKASD IELDQSDEWA TFYNARFEVL DVPIFYLPYV TVPVGDTRKT GVLIPSIGLD
     SKNGFELSVP IYWNIAPNYD ATTTINYMER RGTQLETEFR YLTELGKGTV DAEYLNEDDK
     FKDKGSRWGV SWDHSGIYQQ HWKFDVEYSK VSDIDYFQDL NSSIGTRDEG QLQQSGEVSY
     RSQDWDMTMR VRDFQVLVEE QTPYRLMPQI EFNYYAPQFY SEFDFNLHSH ISKFTTDDKA
     KPSATRVHLE PKLSLPLSGT WWSLIPETSL LYTYYQQDFD KQPVGPNGSL NLDHEVSRTI
     PEVRINGAIY LDSTHKFLGE YLQTLEPKIQ YLYVPEVDQS NIYGGTGDGG YDSSKLQLDY
     YGLFRDRQYS GVDYIADANQ FSVGATSRFY DDAYKERMNI SFGQILYLNG SGTEQNNDDK
     NSSAWAMESD FNYDDYLFYH GGIQYDSNVS ELQVANSTLE YRFSKGYIQA NYRYVSKNYI
     ESNVNFEDDL SLITQHGIYQ AGLLSEYNLG RNWALKGQYF HDTKEDQMIE ALVGVTYLSD
     CWSFGLTYSD QLIAPESAKT IGTYEPEYES NLMLSIAIRG LGNNTGITSG SANNALDYGR
     PFYLNN
 
 
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