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RRE1_SYNY3
ID   RRE1_SYNY3              Reviewed;         231 AA.
AC   P72781;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 2.
DT   25-MAY-2022, entry version 149.
DE   RecName: Full=Response regulator Rre1 {ECO:0000303|PubMed:15471853};
GN   Name=rre1 {ECO:0000303|PubMed:15471853}; Synonyms=ycf29;
GN   OrderedLocusNames=slr1783 {ECO:0000312|EMBL:BAA16796.1};
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION IN HYPEROSMOTIC STRESS RESPONSE, REGULON, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=15471853; DOI=10.1074/jbc.m410162200;
RA   Paithoonrangsarid K., Shoumskaya M.A., Kanesaki Y., Satoh S., Tabata S.,
RA   Los D.A., Zinchenko V.V., Hayashi H., Tanticharoen M., Suzuki I.,
RA   Murata N.;
RT   "Five histidine kinases perceive osmotic stress and regulate distinct sets
RT   of genes in Synechocystis.";
RL   J. Biol. Chem. 279:53078-53086(2004).
RN   [3]
RP   FUNCTION IN SALT STRESS RESPONSE, REGULON, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=15805106; DOI=10.1074/jbc.m412174200;
RA   Shoumskaya M.A., Paithoonrangsarid K., Kanesaki Y., Los D.A.,
RA   Zinchenko V.V., Tanticharoen M., Suzuki I., Murata N.;
RT   "Identical Hik-Rre systems are involved in perception and transduction of
RT   salt signals and hyperosmotic signals but regulate the expression of
RT   individual genes to different extents in synechocystis.";
RL   J. Biol. Chem. 280:21531-21538(2005).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=19411329; DOI=10.1128/jb.00183-09;
RA   Vidal R., Lopez-Maury L., Guerrero M.G., Florencio F.J.;
RT   "Characterization of an alcohol dehydrogenase from the Cyanobacterium
RT   Synechocystis sp. strain PCC 6803 that responds to environmental stress
RT   conditions via the Hik34-Rre1 two-component system.";
RL   J. Bacteriol. 191:4383-4391(2009).
RN   [5]
RP   SEQUENCE REVISION TO N-TERMINUS, PHOSPHORYLATED BY HIK2, AND DNA-BINDING.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=25714549; DOI=10.1093/femsle/fnv030;
RA   Vidal R.;
RT   "Identification of the correct form of the mis-annotated response regulator
RT   Rre1 from the cyanobacterium Synechocystis sp. PCC 6803.";
RL   FEMS Microbiol. Lett. 362:0-0(2015).
RN   [6]
RP   INTERACTION WITH HIK2.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=26904089; DOI=10.3389/fpls.2016.00137;
RA   Ibrahim I.M., Puthiyaveetil S., Allen J.F.;
RT   "A Two-Component Regulatory System in Transcriptional Control of
RT   Photosystem Stoichiometry: Redox-Dependent and Sodium Ion-Dependent
RT   Phosphoryl Transfer from Cyanobacterial Histidine Kinase Hik2 to Response
RT   Regulators Rre1 and RppA.";
RL   Front. Plant Sci. 7:137-137(2016).
CC   -!- FUNCTION: Member of at least 2 two-component regulatory systems
CC       Hik2/Rre1 and Hik34/Rre1. Responds to hyperosmotic stress, regulates
CC       expression of at least 24 genes including dnaK2 and hspA with Hik34 and
CC       sigB (sll0306), sll0528, slr1119, slr0852 and ssr3188 with Hik2
CC       (Probable). Responds to salt stress, regulates expression of at least
CC       24 genes including adhA, dnaK2 and hspA with Hik34 (PubMed:15805106,
CC       PubMed:19411329). Binds the adhA promoter (PubMed:19411329).
CC       Phosphorylated by Hik2 in vitro (PubMed:25714549, PubMed:26904089).
CC       Phosphorylated protein has 10-fold higher affinity for DNA than
CC       unphosphorylated protein (PubMed:25714549).
CC       {ECO:0000269|PubMed:15805106, ECO:0000269|PubMed:19411329,
CC       ECO:0000269|PubMed:25714549, ECO:0000269|PubMed:26904089,
CC       ECO:0000305|PubMed:15471853}.
CC   -!- SUBUNIT: Interacts with histidine kinase Hik2; may accept phosphate
CC       from Hik2. {ECO:0000269|PubMed:26904089}.
CC   -!- DISRUPTION PHENOTYPE: Loss or reduction of expression of about 30 genes
CC       in response to hyperosmotic (0.5 M sorbitol) or salt (0.5 M NaCl)
CC       stress. Most of these genes encode known heat-shock proteins.
CC       {ECO:0000269|PubMed:15471853, ECO:0000269|PubMed:15805106,
CC       ECO:0000269|PubMed:19411329}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA16796.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305|PubMed:25714549};
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DR   EMBL; BA000022; BAA16796.1; ALT_INIT; Genomic_DNA.
DR   PIR; S74644; S74644.
DR   AlphaFoldDB; P72781; -.
DR   SMR; P72781; -.
DR   IntAct; P72781; 4.
DR   STRING; 1148.1651869; -.
DR   PaxDb; P72781; -.
DR   EnsemblBacteria; BAA16796; BAA16796; BAA16796.
DR   KEGG; syn:slr1783; -.
DR   eggNOG; COG2197; Bacteria.
DR   InParanoid; P72781; -.
DR   PhylomeDB; P72781; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..231
FT                   /note="Response regulator Rre1"
FT                   /id="PRO_0000453143"
FT   DOMAIN          6..123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          163..228
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   DNA_BIND        187..206
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   231 AA;  25767 MW;  2F62900E1EDBEEFC CRC64;
     MAEPISLLLV DDEPGVRESV QAFLEDSGDF KVDLAANATE AWDYLQHHLP ALVISDIMMP
     QVDGYQFLQK LREDARFQSL PVVFLTARGM TGDRIQGYQT GCDAFLSKPF DPDELEAIVR
     NLLARQQASS DAGSESAKLQ EIYQEIRALK EQIGQPSGIH TTPSPIKLDF TPREQSVLDL
     VSQGLMNKEI AAQLKTSVRN VEKYVSRLFT KTGTNSRTEL VRFALQHGLT E
 
 
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