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CSRA_CAMJ8
ID   CSRA_CAMJ8              Reviewed;          75 AA.
AC   P0DPD4;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN   Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167}; OrderedLocusNames=C8J_1044;
OS   Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS   11828).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=407148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81116 / NCTC 11828;
RX   PubMed=17873037; DOI=10.1128/jb.01404-07;
RA   Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA   van Vliet A.H.M.;
RT   "The complete genome sequence of Campylobacter jejuni strain 81116
RT   (NCTC11828).";
RL   J. Bacteriol. 189:8402-8403(2007).
RN   [2]
RP   FUNCTION, INTERACTION WITH FLIW, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=81116 / NCTC 11828;
RX   PubMed=27353476; DOI=10.1111/mmi.13455;
RA   Radomska K.A., Ordonez S.R., Woesten M.M., Wagenaar J.A., van Putten J.P.;
RT   "Feedback control of Campylobacter jejuni flagellin levels through
RT   reciprocal binding of FliW to flagellin and the global regulator CsrA.";
RL   Mol. Microbiol. 102:207-220(2016).
CC   -!- FUNCTION: A translational regulator that binds mRNA to regulate
CC       translation initiation and/or mRNA stability. Usually binds in the 5'-
CC       UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding,
CC       thus repressing translation. Its function is probably anatagonized by
CC       FliW. Inhibits translation of flaA mRNA in vitro (PubMed:27353476).
CC       Involved in post-transcriptional regulation of flagellin biosynthesis
CC       (PubMed:27353476). {ECO:0000269|PubMed:27353476,
CC       ECO:0000305|PubMed:27353476}.
CC   -!- SUBUNIT: Homodimer; the beta-strands of each monomer intercalate to
CC       form a hydrophobic core, while the alpha-helices form wings that extend
CC       away from the core (By similarity). Interacts with FliW
CC       (PubMed:27353476). {ECO:0000255|HAMAP-Rule:MF_00167,
CC       ECO:0000269|PubMed:27353476}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
CC   -!- DISRUPTION PHENOTYPE: Increased levels of flagellins FlaA and FlaB
CC       (PubMed:27353476). In double csrA-fliW deletions flagellin levels are
CC       slightly lower than wild-type (PubMed:27353476).
CC       {ECO:0000269|PubMed:27353476}.
CC   -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00167}.
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DR   EMBL; CP000814; ABV52643.1; -; Genomic_DNA.
DR   RefSeq; WP_002852854.1; NC_009839.1.
DR   AlphaFoldDB; P0DPD4; -.
DR   SMR; P0DPD4; -.
DR   KEGG; cju:C8J_1044; -.
DR   HOGENOM; CLU_164837_0_2_7; -.
DR   OMA; RDESIMI; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:1902208; P:regulation of bacterial-type flagellum assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.4380; -; 1.
DR   HAMAP; MF_00167; CsrA; 1.
DR   InterPro; IPR003751; CsrA.
DR   InterPro; IPR036107; CsrA_sf.
DR   PANTHER; PTHR34984; PTHR34984; 1.
DR   Pfam; PF02599; CsrA; 1.
DR   SUPFAM; SSF117130; SSF117130; 1.
DR   TIGRFAMs; TIGR00202; csrA; 1.
PE   1: Evidence at protein level;
KW   Bacterial flagellum biogenesis; Cytoplasm; Repressor; RNA-binding;
KW   Translation regulation.
FT   CHAIN           1..75
FT                   /note="Translational regulator CsrA"
FT                   /id="PRO_0000442734"
SQ   SEQUENCE   75 AA;  8441 MW;  B353436EC460C031 CRC64;
     MLILSRKENE SIIIGEGIEI KVVQTGKGYA KIGIEAPKSL MILRKELVQQ VKDENLHSVV
     QNDIKLDDLS KKLIK
 
 
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