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RCP1_SYNY3
ID   RCP1_SYNY3              Reviewed;         147 AA.
AC   Q55169;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Response regulator Rcp1;
GN   Name=rcp1; OrderedLocusNames=slr0474;
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=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
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   [3]
RP   PHOSPHORYLATION AT ASP-68, AND MUTAGENESIS OF ASP-68.
RX   PubMed=9278513; DOI=10.1126/science.277.5331.1505;
RA   Yeh K.-C., Wu S.-H., Murphy J.T., Lagarias J.C.;
RT   "A cyanobacterial phytochrome two-component light sensory system.";
RL   Science 277:1505-1508(1997).
CC   -!- FUNCTION: Forms a two-component system with Cph1 in which it acts as
CC       receiver substrate.
CC   -!- INTERACTION:
CC       Q55169; Q55168: cph1; NbExp=2; IntAct=EBI-766949, EBI-594457;
CC   -!- PTM: Phosphorylated by Cph1. {ECO:0000269|PubMed:9278513}.
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DR   EMBL; BA000022; BAA10308.1; -; Genomic_DNA.
DR   PIR; S74390; S74390.
DR   PDB; 1I3C; X-ray; 1.90 A; A/B=1-147.
DR   PDB; 1JLK; X-ray; 2.30 A; A/B=1-147.
DR   PDBsum; 1I3C; -.
DR   PDBsum; 1JLK; -.
DR   AlphaFoldDB; Q55169; -.
DR   SMR; Q55169; -.
DR   IntAct; Q55169; 4.
DR   STRING; 1148.1001166; -.
DR   PaxDb; Q55169; -.
DR   EnsemblBacteria; BAA10308; BAA10308; BAA10308.
DR   KEGG; syn:slr0474; -.
DR   eggNOG; COG0784; Bacteria.
DR   InParanoid; Q55169; -.
DR   OMA; FEKFWFS; -.
DR   PhylomeDB; Q55169; -.
DR   EvolutionaryTrace; Q55169; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Reference proteome;
KW   Two-component regulatory system.
FT   CHAIN           1..147
FT                   /note="Response regulator Rcp1"
FT                   /id="PRO_0000081208"
FT   DOMAIN          10..135
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         68
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT                   ECO:0000269|PubMed:9278513"
FT   MUTAGEN         68
FT                   /note="D->A: Unable to be phosphorylated by cph1."
FT                   /evidence="ECO:0000269|PubMed:9278513"
FT   STRAND          9..14
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   HELIX           18..29
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   STRAND          35..40
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   HELIX           43..50
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   HELIX           76..85
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   TURN            87..91
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   STRAND          94..99
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   HELIX           103..111
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   HELIX           124..138
FT                   /evidence="ECO:0007829|PDB:1I3C"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:1I3C"
SQ   SEQUENCE   147 AA;  16609 MW;  C854E8036C9FD58E CRC64;
     MSDESNPPKV ILLVEDSKAD SRLVQEVLKT STIDHELIIL RDGLAAMAFL QQQGEYENSP
     RPNLILLDLN LPKKDGREVL AEIKQNPDLK RIPVVVLTTS HNEDDVIASY ELHVNCYLTK
     SRNLKDLFKM VQGIESFWLE TVTLPAA
 
 
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