(data stored in SCRATCH zone)

SWISSPROT: CSRA_BACSU

ID   CSRA_BACSU              Reviewed;          74 AA.
AC   P33911;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   11-DEC-2019, entry version 125.
DE   RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN   Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN   Synonyms=sow {ECO:0000303|PubMed:21895793}, yviG;
GN   OrderedLocusNames=BSU35370;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2498284; DOI=10.1128/jb.171.6.3095-3101.1989;
RA   Mirel D.B., Chamberlin M.J.;
RT   "The Bacillus subtilis flagellin gene (hag) is transcribed by the sigma 28
RT   form of RNA polymerase.";
RL   J. Bacteriol. 171:3095-3101(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969505; DOI=10.1099/13500872-142-11-3079;
RA   Soldo B., Lazarevic V., Mauel C., Karamata D.;
RT   "Sequence of the 305 degrees-307 degrees region of the Bacillus subtilis
RT   chromosome.";
RL   Microbiology 142:3079-3088(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   IDENTIFICATION.
RA   Robison K.;
RL   Unpublished observations (SEP-1993).
RN   [5]
RP   FUNCTION IN TRANSLATION REPRESSION, SUBUNIT, INDUCTION, DISRUPTION
RP   PHENOTYPE, AND RNA-BINDING.
RC   STRAIN=168, and 1A96;
RX   PubMed=17555441; DOI=10.1111/j.1365-2958.2007.05765.x;
RA   Yakhnin H., Pandit P., Petty T.J., Baker C.S., Romeo T., Babitzke P.;
RT   "CsrA of Bacillus subtilis regulates translation initiation of the gene
RT   encoding the flagellin protein (hag) by blocking ribosome binding.";
RL   Mol. Microbiol. 64:1605-1620(2007).
RN   [6]
RP   FUNCTION IN TRANSLATION REPRESSION, INTERACTION WITH FLIW, DISRUPTION
RP   PHENOTYPE, MUTAGENESIS OF ARG-6; LYS-7; VAL-25; LEU-32; GLY-33; ALA-36 AND
RP   GLU-46, AND RNA-BINDING.
RC   STRAIN=3610;
RX   PubMed=21895793; DOI=10.1111/j.1365-2958.2011.07822.x;
RA   Mukherjee S., Yakhnin H., Kysela D., Sokoloski J., Babitzke P.,
RA   Kearns D.B.;
RT   "CsrA-FliW interaction governs flagellin homeostasis and a checkpoint on
RT   flagellar morphogenesis in Bacillus subtilis.";
RL   Mol. Microbiol. 82:447-461(2011).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=3610;
RX   PubMed=23144244; DOI=10.1128/jb.01654-12;
RA   Mukherjee S., Babitzke P., Kearns D.B.;
RT   "FliW and FliS function independently to control cytoplasmic flagellin
RT   levels in Bacillus subtilis.";
RL   J. Bacteriol. 195:297-306(2013).
RN   [8]
RP   FUNCTION, INTERACTION WITH FLIW, DOMAIN, AND MUTAGENESIS OF ARG-6; LYS-7;
RP   ILE-14; GLY-33; ALA-36; GLU-46; LEU-49; ASN-55 AND ALA-58.
RC   STRAIN=3610;
RX   PubMed=27516547; DOI=10.1073/pnas.1602455113;
RA   Mukherjee S., Oshiro R.T., Yakhnin H., Babitzke P., Kearns D.B.;
RT   "FliW antagonizes CsrA RNA binding by a noncompetitive allosteric
RT   mechanism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9870-9875(2016).
RN   [9]
RP   REVIEW.
RX   PubMed=25833324; DOI=10.1128/mmbr.00052-14;
RA   Vakulskas C.A., Potts A.H., Babitzke P., Ahmer B.M., Romeo T.;
RT   "Regulation of bacterial virulence by Csr (Rsm) systems.";
RL   Microbiol. Mol. Biol. Rev. 79:193-224(2015).
RN   [10]
RP   STRUCTURE BY NMR.
RA   Koharudin L.M.I., Georgiou T., Kleanthous C., Geoffrey R., Kaptein R.,
RA   Boelens R.;
RT   "A model for RNA binding by the bacterial carbon storage regulatory
RT   protein, csrA.";
RL   Submitted (OCT-2005) to the PDB data bank.
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. Represses expression of flagellin (hag) in
CC       a post-transcriptional fashion. Specifically binds to 2 sites in the
CC       5'-UTR of hag mRNA in a cooperative fashion; the second site overlaps
CC       the Shine-Dalgarno sequence and prevents 30S ribosomal subunit binding
CC       (PubMed:17555441). Mutation of either binding site abolishes CsrA
CC       regulation of hag expression (PubMed:17555441, PubMed:21895793).
CC       Repression is greater in the 1A96 than 168 genetic background and
CC       higher in minimal than rich medium (PubMed:17555441). Translation
CC       repression is antagonized by FliW (PubMed:21895793). Partner switching
CC       by flagellin between FliW and CsrA provides a flagellar assembly
CC       checkpoint to tightly control the timing of flagellin synthesis.
CC       Flagellin binds to assembly factor FliW, freeing CsrA to repress
CC       translation of the flagellin mRNA. When the flagellar hook is assembled
CC       flagellin is secreted, depleting intracellular flagellin, which frees
CC       FliW to interact with CsrA and inhibits CsrA binding to mRNA. This
CC       derepresses flagellin translation and provides protein for flagellar
CC       assembly. Once the flagellar filament is completed cytoplasmic
CC       flagellin levels rise and CsrA translation repression of flagellin
CC       reinitiates (PubMed:21895793, PubMed:27516547). Overexpression leads to
CC       a dramatic reduction in motility, a significant reduction in flagellin
CC       synthesis and reduced flagella assembly (PubMed:21895793).
CC       {ECO:0000269|PubMed:17555441, ECO:0000269|PubMed:21895793,
CC       ECO:0000269|PubMed:27516547}.
CC   -!- SUBUNIT: Homodimer (PubMed:17555441). The beta-strands of each monomer
CC       intercalate to form a hydrophobic core while the alpha-helices form
CC       wings that extend away from the core (By similarity). Two molecules of
CC       FliW interact with 1 homodimer (PubMed:21895793, PubMed:27516547). mRNA
CC       and FliW bind to different sites on CsrA (PubMed:27516547).
CC       {ECO:0000250|UniProtKB:O69078, ECO:0000269|PubMed:21895793,
CC       ECO:0000269|PubMed:27516547, ECO:0000305|PubMed:17555441}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
CC   -!- INDUCTION: Part of the SigD-controlled yvyF-csrA operon and the SigA-
CC       controlled fliW-csrA operon (PubMed:17555441). Expressed from the SigA
CC       operon at low levels during log phase, with a 5-fold increase as the
CC       culture transitions to stationary phase, peaking 1 hour later.
CC       {ECO:0000269|PubMed:17555441}.
CC   -!- DOMAIN: Contacts FliW via its C-terminus (residues 49-58).
CC       {ECO:0000269|PubMed:27516547}.
CC   -!- DISRUPTION PHENOTYPE: Increased expression of flagellin (hag), 30%
CC       decrease in motility halo (PubMed:17555441). Suppresses the motility
CC       loss and flagellar assembly defect of an fliW deletion
CC       (PubMed:21895793). Suppresses the phenotypes associated with deletion
CC       of the intracellular flagella chaperone fliS (PubMed:23144244).
CC       {ECO:0000269|PubMed:17555441, ECO:0000269|PubMed:21895793,
CC       ECO:0000269|PubMed:23144244}.
CC   -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00167}.
DR   EMBL; M26948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U56901; AAC44950.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15554.1; -; Genomic_DNA.
DR   PIR; H69608; H69608.
DR   RefSeq; NP_391417.1; NC_000964.3.
DR   RefSeq; WP_003219727.1; NZ_JNCM01000033.1.
DR   PDB; 1T3O; NMR; -; A=1-74.
DR   PDBsum; 1T3O; -.
DR   SMR; P33911; -.
DR   STRING; 224308.BSU35370; -.
DR   PaxDb; P33911; -.
DR   PRIDE; P33911; -.
DR   EnsemblBacteria; CAB15554; CAB15554; BSU35370.
DR   GeneID; 936731; -.
DR   KEGG; bsu:BSU35370; -.
DR   PATRIC; fig|224308.179.peg.3828; -.
DR   eggNOG; ENOG41085Y9; Bacteria.
DR   eggNOG; COG1551; LUCA.
DR   HOGENOM; HOG000020767; -.
DR   InParanoid; P33911; -.
DR   KO; K03563; -.
DR   OMA; IHRKEVY; -.
DR   PhylomeDB; P33911; -.
DR   BioCyc; BSUB:BSU35370-MONOMER; -.
DR   EvolutionaryTrace; P33911; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IBA:GO_Central.
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; 3.30.70.1680; -; 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;
DR   PRODOM; P33911.
DR   SWISS-2DPAGE; P33911.
KW   3D-structure; Cytoplasm; Reference proteome; Repressor; RNA-binding;
KW   Translation regulation.
FT   CHAIN           1..74
FT                   /note="Translational regulator CsrA"
FT                   /id="PRO_0000177049"
FT   MUTAGEN         6
FT                   /note="R->L,W: In sow-2 and sow28; suppresses the motility
FT                   loss and flagellar assembly defect of an fliW deletion.
FT                   Binds FliW."
FT                   /evidence="ECO:0000269|PubMed:21895793,
FT                   ECO:0000269|PubMed:27516547"
FT   MUTAGEN         7
FT                   /note="K->E: In sow-12; suppresses the motility loss and
FT                   flagellar assembly defect of an fliW deletion. Binds FliW."
FT                   /evidence="ECO:0000269|PubMed:21895793,
FT                   ECO:0000269|PubMed:27516547"
FT   MUTAGEN         14
FT                   /note="I->M: Inhibits motility and flagellar filament
FT                   assembly, still binds FliW. Binds 5'-UTR of hag mRNA, is
FT                   not completed by FliW."
FT                   /evidence="ECO:0000269|PubMed:27516547"
FT   MUTAGEN         25
FT                   /note="V->G: In sow-20; suppresses the motility loss and
FT                   flagellar assembly defect of an fliW deletion."
FT                   /evidence="ECO:0000269|PubMed:21895793"
FT   MUTAGEN         32
FT                   /note="L->P: In sow-10; suppresses the motility loss and
FT                   flagellar assembly defect of an fliW deletion."
FT                   /evidence="ECO:0000269|PubMed:21895793"
FT   MUTAGEN         33
FT                   /note="G->R: In sow-11; suppresses the motility loss and
FT                   flagellar assembly defect of an fliW deletion. Binds FliW."
FT                   /evidence="ECO:0000269|PubMed:21895793,
FT                   ECO:0000269|PubMed:27516547"
FT   MUTAGEN         36
FT                   /note="A->T,V: In sow-8 and sow-4; suppresses the motility
FT                   loss and flagellar assembly defect of an fliW deletion.
FT                   Binds FliW."
FT                   /evidence="ECO:0000269|PubMed:21895793,
FT                   ECO:0000269|PubMed:27516547"
FT   MUTAGEN         46
FT                   /note="E->K: In sow-15; suppresses the motility loss and
FT                   flagellar assembly defect of an fliW deletion. Binds FliW."
FT                   /evidence="ECO:0000269|PubMed:21895793,
FT                   ECO:0000269|PubMed:27516547"
FT   MUTAGEN         49
FT                   /note="L->S: Inhibits motility and flagellar filament
FT                   assembly, reduced binding of FliW."
FT                   /evidence="ECO:0000269|PubMed:27516547"
FT   MUTAGEN         55
FT                   /note="N->D: Inhibits motility and flagellar filament
FT                   assembly, greatly reduced binding of FliW. Binds 5'-UTR of
FT                   hag mRNA, is not completed by FliW."
FT                   /evidence="ECO:0000269|PubMed:27516547"
FT   MUTAGEN         58
FT                   /note="A->V: Inhibits motility and flagellar filament
FT                   assembly, reduced binding of FliW."
FT                   /evidence="ECO:0000269|PubMed:27516547"
FT   STRAND          1..5
FT                   /evidence="ECO:0000244|PDB:1T3O"
FT   STRAND          12..14
FT                   /evidence="ECO:0000244|PDB:1T3O"
FT   TURN            15..17
FT                   /evidence="ECO:0000244|PDB:1T3O"
FT   STRAND          18..20
FT                   /evidence="ECO:0000244|PDB:1T3O"
FT   STRAND          30..38
FT                   /evidence="ECO:0000244|PDB:1T3O"
FT   TURN            52..54
FT                   /evidence="ECO:0000244|PDB:1T3O"
SQ   SEQUENCE   74 AA;  8136 MW;  10E82DA62D3174B5 CRC64;
     MLVLSRKINE AIQIGADIEV KVIAVEGDQV KLGIDAPKHI DIHRKEIYLT IQEENNRAAA
     LSSDVISALS SQKK
//

If you have problems or comments...

PBIL Back to PBIL home page