ID H8Z1A8_9GAMM Unreviewed; 111 AA.
AC H8Z1A8;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Translational regulator CsrA {ECO:0000256|HAMAP-Rule:MF_00167};
DE AltName: Full=Carbon storage regulator {ECO:0000256|HAMAP-Rule:MF_00167};
GN Name=csrA {ECO:0000256|HAMAP-Rule:MF_00167};
GN ORFNames=Thi970DRAFT_01631 {ECO:0000313|EMBL:EIC21423.1};
OS Thiorhodovibrio frisius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodovibrio.
OX NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC21423.1, ECO:0000313|Proteomes:UP000002964};
RN [1] {ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Overmann J.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIC21423.1, ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|EMBL:EIC21423.1,
RC ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Overmann J., Frigaard N.-U., Bryant D., Woyke T.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A key translational regulator that binds mRNA to regulate
CC translation initiation and/or mRNA stability. Mediates global changes
CC in gene expression, shifting from rapid growth to stress survival by
CC linking envelope stress, the stringent response and the catabolite
CC repression systems. Usually binds in the 5'-UTR; binding at or near the
CC Shine-Dalgarno sequence prevents ribosome-binding, repressing
CC translation, binding elsewhere in the 5'-UTR can activate translation
CC and/or stabilize the mRNA. Its function is antagonized by small RNA(s).
CC {ECO:0000256|HAMAP-Rule:MF_00167}.
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. {ECO:0000256|HAMAP-Rule:MF_00167}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00167}.
CC -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000256|HAMAP-
CC Rule:MF_00167}.
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DR EMBL; JH603169; EIC21423.1; -; Genomic_DNA.
DR AlphaFoldDB; H8Z1A8; -.
DR HOGENOM; CLU_2157235_0_0_6; -.
DR Proteomes; UP000002964; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:UniProtKB-UniRule.
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:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.4380; Translational regulator CsrA; 1.
DR HAMAP; MF_00167; CsrA; 1.
DR InterPro; IPR003751; CsrA.
DR InterPro; IPR036107; CsrA_sf.
DR Pfam; PF02599; CsrA; 1.
DR SUPFAM; SSF117130; CsrA-like; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_00167};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00167};
KW Reference proteome {ECO:0000313|Proteomes:UP000002964};
KW Repressor {ECO:0000256|HAMAP-Rule:MF_00167};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00167};
KW Translation regulation {ECO:0000256|HAMAP-Rule:MF_00167}.
FT REGION 74..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 111 AA; 12496 MW; 33BDC25CAD942871 CRC64;
MPNTPQNNDT SRSVGLILTR RPGELIMLEL PEDLGGHRVQ ISCVAIDRNQ VKIGIRAPND
WNIYRGELRG EYVDTGGEAP EADVEAQAPG VTSDRQQIII RTRPRRRRKQ P
//
