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RPPA_SYNY3
ID   RPPA_SYNY3              Reviewed;         234 AA.
AC   Q55933;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 154.
DE   RecName: Full=Response regulator RppA {ECO:0000303|PubMed:10894737};
DE   AltName: Full=Regulator of nickel resistance operon NrsR {ECO:0000303|PubMed:11849552};
DE   AltName: Full=Regulator of photosynthesis- and photopigment-related gene expression {ECO:0000303|PubMed:10894737};
GN   Name=rppA {ECO:0000303|PubMed:10894737};
GN   Synonyms=nrsR {ECO:0000303|PubMed:11849552};
GN   OrderedLocusNames=sll0797 {ECO:0000312|EMBL:BAA10698.1};
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 PHOTOSYSTEM BALANCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=10894737; DOI=10.1128/jb.182.15.4268-4277.2000;
RA   Li H., Sherman L.A.;
RT   "A redox-responsive regulator of photosynthesis gene expression in the
RT   cyanobacterium Synechocystis sp. Strain PCC 6803.";
RL   J. Bacteriol. 182:4268-4277(2000).
RN   [3]
RP   FUNCTION IN NICKEL RESPONSE, INDUCTION BY NI(2+), OPERON, DOMAIN,
RP   DISRUPTION PHENOTYPE, AND DNA-BINDING.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=11849552; DOI=10.1046/j.1365-2958.2002.02741.x;
RA   Lopez-Maury L., Garcia-Dominguez M., Florencio F.J., Reyes J.C.;
RT   "A two-component signal transduction system involved in nickel sensing in
RT   the cyanobacterium Synechocystis sp. PCC 6803.";
RL   Mol. Microbiol. 43:247-256(2002).
RN   [4]
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 two-component regulatory system RppA/RppB, involved
CC       in the establishment of the appropriate stoichiometry between the 2
CC       photosystems. It senses changes in the plastoquinone (PQ) redox poise
CC       (PubMed:10894737). Another group shows this two-component pair, renamed
CC       NrsR/NrsS, controls the nickel-dependent expression of the nrsBACD
CC       operon; they suggest the photosystem-related activities seen earlier
CC       are due to the expression of NrsS (RppB) in the absence of its natural
CC       substrate NrsR (RppA) (PubMed:11849552). May accept phosphate from Hik2
CC       in a possible Hik2/RppA two-component system (Probable).
CC       {ECO:0000269|PubMed:10894737, ECO:0000269|PubMed:11849552,
CC       ECO:0000305|PubMed:26904089}.
CC   -!- SUBUNIT: Interacts with histidine kinase Hik2; may accept phosphate
CC       from Hik2. {ECO:0000269|PubMed:26904089}.
CC   -!- INDUCTION: Expression of the rrpa-rrpB (nrsR-nrsS) operon is induced 3-
CC       fold by Ni(2+) and less by Co(2+). Autoregulates its own expression.
CC       {ECO:0000269|PubMed:11849552}.
CC   -!- DOMAIN: The N-terminal response regulatory domain inhibits DNA-binding
CC       by the rest of the protein, in its absence the protein binds
CC       specifically to the nrsRS-nrsBACD (slr0793-slr0796) intergenic region.
CC       {ECO:0000269|PubMed:11849552}.
CC   -!- DISRUPTION PHENOTYPE: Grows faster than wild-type photomixotrophically
CC       (in light with glucose), specific activity of photosystem II (PSII) is
CC       about 30% higher, most cells are single when 90% of wild-type are
CC       doublets. Increased transcription of most PSII genes under most
CC       conditions, transcription of PSI and phycobilisome-related genes are
CC       mostly decreased (PubMed:10894737). A double rppA-rppB (nrsR-nrsS)
CC       deletion is less tolerant to growth on Ni(2+), no longer expresses nrsB
CC       (slr0793, involved in Ni(2+) resistance) in response to Ni(2+). Loss of
CC       expression of this operon. There are no growth effects, no changes in
CC       pigment concentration, no changes in PSII or nblA transcript levels
CC       seen in the double mutant (PubMed:11849552).
CC       {ECO:0000269|PubMed:10894737, ECO:0000269|PubMed:11849552}.
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DR   EMBL; BA000022; BAA10698.1; -; Genomic_DNA.
DR   PIR; S77006; S77006.
DR   AlphaFoldDB; Q55933; -.
DR   SMR; Q55933; -.
DR   IntAct; Q55933; 3.
DR   STRING; 1148.1001817; -.
DR   PaxDb; Q55933; -.
DR   EnsemblBacteria; BAA10698; BAA10698; BAA10698.
DR   KEGG; syn:sll0797; -.
DR   eggNOG; COG0745; Bacteria.
DR   InParanoid; Q55933; -.
DR   OMA; FIDHPQR; -.
DR   PhylomeDB; Q55933; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR   GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48111; PTHR48111; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 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..234
FT                   /note="Response regulator RppA"
FT                   /id="PRO_0000453145"
FT   DOMAIN          2..118
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        126..232
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   234 AA;  26663 MW;  89DFA614A257162F CRC64;
     MRILLVEDET DLGMAIKKVL VSEKYVVDWV TDGSQAWDYL ENQWTEYTLA IVDWLLPGLS
     GLELCQKLRT QGNSLPVLML TALGEPENRV EGLDAGADDY LTKPFVMAEL LARLRALQRR
     SPQFQPQILT LGNFSLDPSN NLLSVTISEP LNLERQEIAL TVREFQIFQY LMQNPERIIS
     GSKIRQQLWD LDEEPMSNVV AAQMRLIRRK LAQQNCPCPI KTVPGQGYRF TLSP
 
 
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