GenomeNet

Database: UniProt
Entry: A0A0W0YZC1_LEGSP
LinkDB: A0A0W0YZC1_LEGSP
Original site: A0A0W0YZC1_LEGSP 
ID   A0A0W0YZC1_LEGSP        Unreviewed;        98 AA.
AC   A0A0W0YZC1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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_2 {ECO:0000313|EMBL:KTD62184.1};
GN   Synonyms=csrA {ECO:0000256|HAMAP-Rule:MF_00167};
GN   ORFNames=Lspi_2034 {ECO:0000313|EMBL:KTD62184.1};
OS   Legionella spiritensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=452 {ECO:0000313|EMBL:KTD62184.1, ECO:0000313|Proteomes:UP000054877};
RN   [1] {ECO:0000313|EMBL:KTD62184.1, ECO:0000313|Proteomes:UP000054877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD62184.1,
RC   ECO:0000313|Proteomes:UP000054877};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTD62184.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LNYX01000030; KTD62184.1; -; Genomic_DNA.
DR   RefSeq; WP_058483951.1; NZ_LT906457.1.
DR   AlphaFoldDB; A0A0W0YZC1; -.
DR   STRING; 452.Lspi_2034; -.
DR   PATRIC; fig|452.5.peg.2239; -.
DR   OrthoDB; 9809061at2; -.
DR   Proteomes; UP000054877; 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   PANTHER; PTHR34984; CARBON STORAGE REGULATOR; 1.
DR   PANTHER; PTHR34984:SF1; CARBON STORAGE REGULATOR; 1.
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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00167};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054877};
KW   Repressor {ECO:0000256|HAMAP-Rule:MF_00167};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00167};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW   Rule:MF_00167}.
SQ   SEQUENCE   98 AA;  11649 MW;  2B232A0964DCCA64 CRC64;
     MLVLTRRIGE SVVIGEDVYC TIVGYRDGEI RLAFDAPKSL PIHRDEIQRR IYRERQNDNW
     FYDRGAEKES IVDRLINKFK QGHWSTEPKL HSQEQPYA
//
DBGET integrated database retrieval system