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LPTD_BURP1
ID   LPTD_BURP1              Reviewed;         787 AA.
AC   Q3JVW9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=BURPS1710b_0871;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000124; ABA49774.1; -; Genomic_DNA.
DR   RefSeq; WP_004189876.1; NC_007434.1.
DR   AlphaFoldDB; Q3JVW9; -.
DR   SMR; Q3JVW9; -.
DR   EnsemblBacteria; ABA49774; ABA49774; BURPS1710b_0871.
DR   GeneID; 56596647; -.
DR   KEGG; bpm:BURPS1710b_0871; -.
DR   HOGENOM; CLU_009039_0_0_4; -.
DR   OMA; DYSHLDW; -.
DR   OrthoDB; 100018at2; -.
DR   Proteomes; UP000002700; 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   Pfam; PF04453; LptD; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Membrane; Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           40..787
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_0000281594"
SQ   SEQUENCE   787 AA;  86453 MW;  41955832D4CB01EA CRC64;
     MPPKTLFPLV PACDAAPRKK RLAVALLAVP GLVPAVSQAQ LSGAAAEPQA FGSPWDLRLA
     PQLDEHPQKQ GGKPATFVLA DHTNGTAEQD LAAKGAAEIR RGNAAVKADA IHYDQDTDMA
     DAYGKVTVAN GGTTFSGPEA HLKVEANQGF MTTPKYRFTA TGGTGSAERV QLLDSERSVF
     TNGTYTGCQC STNPAWYIKG SEFDFDTGAD EGVARNGVLF FQGVPLFGSP WLTFPLSGDR
     RSGFLPPTFS PFSSTNGFEL SLPYYFNIAP NRDLTITPHI ISKRGIFTQA TFRYLSTNYS
     GTLTGEYLPD DRVAHRNRYA IFWQHQQNFG NGFGGYVYYN KVSDNLYPEE LGSTNQFVNG
     VQTVYQQEAG LTYNNGPWSV LGRYQHWQTL PPSAAPYGRE PQLNVKYTKY NVGGFDFGAE
     ADYSRFRITT ADQPEGDRVM FNPYVSYGLY GPGYFFVPKA QLHMASYDLT TTTGGVPGQP
     KRFTYSIPTL SLDTGLVFDR SVRLFGQDFI QTLEPRLFYV YTPYRNQSNA PLFDTAVSDF
     GLAEIFTPNT FVGNDRIADA NRLTAALTTR FINPTTGDER ARFVIAQQYY FTDQRVTLLP
     TEAPATARHS DLILGASVKL GAGFASETAF QYNVDNNQLV KSSVGFGYSP GERRVINVGY
     RYTRQNPTLS NEPINQILMS AQWPLTRRLY AVGRLNYDLA SSRVVDGLVG FQYDADCWAF
     GVGVQRYANG LNSSGQQNSS TRVLAQLVLK GLTSIDNGLV TAFRAGVQGY TPLPPAPAPL
     SRFSNYD
 
 
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