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LPTD_ACTP2
ID   LPTD_ACTP2              Reviewed;         778 AA.
AC   A3N0X0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=APL_0962;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN74056.1; -; Genomic_DNA.
DR   RefSeq; WP_005610226.1; NC_009053.1.
DR   AlphaFoldDB; A3N0X0; -.
DR   SMR; A3N0X0; -.
DR   STRING; 416269.APL_0962; -.
DR   PRIDE; A3N0X0; -.
DR   EnsemblBacteria; ABN74056; ABN74056; APL_0962.
DR   KEGG; apl:APL_0962; -.
DR   eggNOG; COG1452; Bacteria.
DR   HOGENOM; CLU_009039_2_0_6; -.
DR   OMA; DYSHLDW; -.
DR   Proteomes; UP000001432; Chromosome.
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..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01411"
FT   CHAIN           24..778
FT                   /note="LPS-assembly protein LptD"
FT                   /id="PRO_1000087384"
SQ   SEQUENCE   778 AA;  89823 MW;  8FDB843343B9FBDE CRC64;
     MKTRYSVLSV AMTAAFYTQY AQADLREQCL LGVPHFQGEE VTGDQTMMPI EIEADNAVIN
     QPKDATYTGD VAIKQGNRSL FADEVRVEQN GEQERRAFLK GSYRYQDNLI QAHGRDAAMD
     LGSETAELQN TEFQLVGRQG RGTAESGSFN HNKRILKNAT FTACLPNDNA WSIEGNEMIQ
     HIDEEYAEIW HARFKVLGMP VFYSPYLQFP IGDRRRSGLL IPNFHRSSKD GFAYSQPFYW
     NIAPNMDATI TPTYYSRRGW QISPEYRYLT KLGEGIVAGE YIGKDRLDEY RPDDNDRKRY
     LMHWRHNMSF LTGWRLYVDY TKVSDKRYFS DFDSEYGSST DGYATQQFKL GYYQPNYNLS
     ISGKKFQTFD ELDVGPYRVL PQIDFNYYND ELVKGGDFKL FAQTARFEND SKLMPKAWRF
     HVEPTLNFPL ANRYGSLNFE TKLYATHYLQ EKGSSKQADD MDKNVTRIIP QVKVDLQTVL
     EADKQLFKGF NQTFEPRVQY VYRPYKDQSN IGSGLNQSVS FGYDSALLQS DYFSLFNDRR
     YSGLDRISSA NLITAGGTNR FFNEKTGVEV FNFSIGQTYY LSPSKIDDLS QNSTTKRSSS
     WALESNWKFH RKWNWHGAYQ YDTRLNQTSL ANTSLQYKPS QDKLVQLSYR FASKDYINQN
     LRSNTYGQDI KQVGAVVGWE LTDRVAFMAS HYHDIALKKP VESQLSVNYN TCCWSANVYV
     ARKLTATPIG SPDTINDLYY DNKFGVNFEL RFGTNYSSGV RKMLKKGMIP YTEQYGIN
 
 
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