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LOLB_THIDA
ID   LOLB_THIDA              Reviewed;         186 AA.
AC   Q3SLR7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Outer-membrane lipoprotein LolB {ECO:0000255|HAMAP-Rule:MF_00233};
DE   Flags: Precursor;
GN   Name=lolB {ECO:0000255|HAMAP-Rule:MF_00233}; OrderedLocusNames=Tbd_0385;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
CC   -!- FUNCTION: Plays a critical role in the incorporation of lipoproteins in
CC       the outer membrane after they are released by the LolA protein.
CC       {ECO:0000255|HAMAP-Rule:MF_00233}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00233}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00233}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00233}.
CC   -!- SIMILARITY: Belongs to the LolB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00233}.
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DR   EMBL; CP000116; AAZ96338.1; -; Genomic_DNA.
DR   RefSeq; WP_011310898.1; NC_007404.1.
DR   AlphaFoldDB; Q3SLR7; -.
DR   SMR; Q3SLR7; -.
DR   STRING; 292415.Tbd_0385; -.
DR   EnsemblBacteria; AAZ96338; AAZ96338; Tbd_0385.
DR   KEGG; tbd:Tbd_0385; -.
DR   eggNOG; COG3017; Bacteria.
DR   HOGENOM; CLU_092816_3_1_4; -.
DR   OMA; YQTRGSF; -.
DR   OrthoDB; 1797257at2; -.
DR   Proteomes; UP000008291; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044874; P:lipoprotein localization to outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd16326; LolB; 1.
DR   HAMAP; MF_00233; LolB; 1.
DR   InterPro; IPR029046; LolA/LolB/LppX.
DR   InterPro; IPR004565; OM_lipoprot_LolB.
DR   Pfam; PF03550; LolB; 1.
DR   SUPFAM; SSF89392; SSF89392; 1.
DR   TIGRFAMs; TIGR00548; lolB; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Chaperone; Lipoprotein; Membrane; Palmitate;
KW   Protein transport; Reference proteome; Signal; Transport.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT   CHAIN           17..186
FT                   /note="Outer-membrane lipoprotein LolB"
FT                   /id="PRO_0000336619"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00233"
SQ   SEQUENCE   186 AA;  19963 MW;  F42ED92FD031E14C CRC64;
     MRRLAVIASL AWALGGCATV APPPQAAIPV PLADAWTLQG RLGVQTERES LSGQIRWQHG
     GGVDQVLLTS PLGQGVARIV RDPEGVSLEL PGQPVRRATD VDTLTRDALG YELPVAGLAW
     WIQARPDPLR EAAVALGDDG RPARIVQDGW TIDYLQYGAD ARPRKLVVSR AGLEIRLVAD
     SWQSAP
 
 
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