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Database: UniProt
Entry: N9ADM3_9GAMM
LinkDB: N9ADM3_9GAMM
Original site: N9ADM3_9GAMM 
ID   N9ADM3_9GAMM            Unreviewed;        84 AA.
AC   N9ADM3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=F950_01999 {ECO:0000313|EMBL:ENV59452.1};
OS   Acinetobacter soli NIPH 2899.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217677 {ECO:0000313|EMBL:ENV59452.1, ECO:0000313|Proteomes:UP000018433};
RN   [1] {ECO:0000313|EMBL:ENV59452.1, ECO:0000313|Proteomes:UP000018433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIPH 2899 {ECO:0000313|EMBL:ENV59452.1,
RC   ECO:0000313|Proteomes:UP000018433};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter soli NIPH 2899.";
RL   Submitted (FEB-2013) 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:ENV59452.1}.
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DR   EMBL; APPV01000011; ENV59452.1; -; Genomic_DNA.
DR   RefSeq; WP_004925987.1; NZ_KB849643.1.
DR   AlphaFoldDB; N9ADM3; -.
DR   SMR; N9ADM3; -.
DR   GeneID; 67510726; -.
DR   PATRIC; fig|1217677.3.peg.1944; -.
DR   HOGENOM; CLU_164837_2_1_6; -.
DR   Proteomes; UP000018433; 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   NCBIfam; TIGR00202; csrA; 1.
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   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}.
FT   REGION          64..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   84 AA;  9830 MW;  CAFB6A627475983B CRC64;
     MLILTRRVGE TLMIGDQVSV TVLGVKGNQV RIGVNAPKEV SVHREEIYQR IQHERAMHEH
     LQHLDQDYQP SFEDDNYSQN NFNR
//
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