PHY1_SYNY3
ID PHY1_SYNY3 Reviewed; 748 AA.
AC Q55168;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Phytochrome-like protein Cph1;
DE EC=2.7.13.3;
DE AltName: Full=Bacteriophytochrome Cph1;
DE AltName: Full=Light-regulated histidine kinase 1;
GN Name=cph1; OrderedLocusNames=slr0473;
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 CHARACTERIZATION.
RX PubMed=9109482; DOI=10.1038/386663a0;
RA Hughes J., Lamparter T., Mittmann F., Hartmann E., Gartner W., Wilde A.,
RA Borner T.;
RT "A prokaryotic phytochrome.";
RL Nature 386:663-663(1997).
RN [4]
RP CHARACTERIZATION, PHOSPHORYLATION AT HIS-538, AND MUTAGENESIS OF HIS-538.
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).
RN [5]
RP CHARACTERIZATION.
RX PubMed=10828948; DOI=10.1021/bi992916s;
RA Park C.-M., Shim J.-Y., Yang S.-S., Kang J.-G., Kim J.-I., Luka Z.,
RA Song P.-S.;
RT "Chromophore-apoprotein interactions in Synechocystis sp. PCC6803
RT phytochrome Cph1.";
RL Biochemistry 39:6349-6356(2000).
RN [6]
RP REVIEW.
RX PubMed=10594094; DOI=10.1104/pp.121.4.1059;
RA Hughes J., Lamparter T.;
RT "Prokaryotes and phytochrome. The connection to chromophores and
RT signaling.";
RL Plant Physiol. 121:1059-1068(1999).
CC -!- FUNCTION: Regulatory photoreceptor which exists in two forms that are
CC reversibly interconvertible by light: the R form that absorbs maximally
CC in the red region of the spectrum and the FR form that absorbs
CC maximally in the far-red region. Has also a slight blue shift for the
CC far-red maximum. Forms a two-component system with the Rrcp1 response
CC regulator.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Q55168; Q55168: cph1; NbExp=8; IntAct=EBI-594457, EBI-594457;
CC Q55168; Q55169: rcp1; NbExp=2; IntAct=EBI-594457, EBI-766949;
CC -!- PTM: Contains one covalently linked tetrapyrrole chromophore.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: The R form exhibits both ATP-dependent
CC autophosphorylation and phosphotransfer to Rcp1 activities. Unlike the
CC higher plants where Pfr is thought to be the active form.
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10307.1; -; Genomic_DNA.
DR PIR; S74389; S74389.
DR PDB; 2VEA; X-ray; 2.21 A; A=1-514.
DR PDB; 3ZQ5; X-ray; 1.95 A; A=1-514.
DR PDBsum; 2VEA; -.
DR PDBsum; 3ZQ5; -.
DR AlphaFoldDB; Q55168; -.
DR SMR; Q55168; -.
DR DIP; DIP-34651N; -.
DR IntAct; Q55168; 10.
DR MINT; Q55168; -.
DR STRING; 1148.1001165; -.
DR iPTMnet; Q55168; -.
DR PaxDb; Q55168; -.
DR EnsemblBacteria; BAA10307; BAA10307; BAA10307.
DR KEGG; syn:slr0473; -.
DR eggNOG; COG4251; Bacteria.
DR InParanoid; Q55168; -.
DR OMA; ECHRGRI; -.
DR PhylomeDB; Q55168; -.
DR BRENDA; 2.7.13.3; 382.
DR EvolutionaryTrace; Q55168; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:UniProtKB.
DR GO; GO:0009883; F:red or far-red light photoreceptor activity; IDA:UniProtKB.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0009585; P:red, far-red light phototransduction; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0009639; P:response to red or far red light; IDA:UniProtKB.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromophore; Kinase; Nucleotide-binding;
KW Phosphoprotein; Photoreceptor protein; Receptor; Reference proteome;
KW Sensory transduction; Transferase.
FT CHAIN 1..748
FT /note="Phytochrome-like protein Cph1"
FT /id="PRO_0000172001"
FT DOMAIN 19..86
FT /note="PAS"
FT DOMAIN 152..320
FT /note="GAF"
FT DOMAIN 535..748
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 87..510
FT /note="Chromophore binding domain"
FT BINDING 259
FT /ligand="a tetrapyrrole"
FT /ligand_id="ChEBI:CHEBI:26932"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
FT MOD_RES 538
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:9278513"
FT MUTAGEN 538
FT /note="H->K: No autophosphorylation; no phosphotransfer to
FT Rcp1."
FT /evidence="ECO:0000269|PubMed:9278513"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 102..112
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 153..168
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:2VEA"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 270..279
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 282..293
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 299..344
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 348..353
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 385..397
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 414..419
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 435..441
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:3ZQ5"
FT HELIX 491..514
FT /evidence="ECO:0007829|PDB:3ZQ5"
SQ SEQUENCE 748 AA; 84233 MW; A9ECA6D8D5B3C88A CRC64;
MATTVQLSDQ SLRQLETLAI HTAHLIQPHG LVVVLQEPDL TISQISANCT GILGRSPEDL
LGRTLGEVFD SFQIDPIQSR LTAGQISSLN PSKLWARVMG DDFVIFDGVF HRNSDGLLVC
ELEPAYTSDN LPFLGFYHMA NAALNRLRQQ ANLRDFYDVI VEEVRRMTGF DRVMLYRFDE
NNHGDVIAED KRDDMEPYLG LHYPESDIPQ PARRLFIHNP IRVIPDVYGV AVPLTPAVNP
STNRAVDLTE SILRSAYHCH LTYLKNMGVG ASLTISLIKD GHLWGLIACH HQTPKVIPFE
LRKACEFFGR VVFSNISAQE DTETFDYRVQ LAEHEAVLLD KMTTAADFVE GLTNHPDRLL
GLTGSQGAAI CFGEKLILVG ETPDEKAVQY LLQWLENREV QDVFFTSSLS QIYPDAVNFK
SVASGLLAIP IARHNFLLWF RPEVLQTVNW GGDPNHAYEA TQEDGKIELH PRQSFDLWKE
IVRLQSLPWQ SVEIQSALAL KKAIVNLILR QAEELAQLAR NLERSNADLK KFAYIASHDL
QEPLNQVSNY VQLLEMRYSE ALDEDAKDFI DFAVTGVSLM QTLIDDILTY AKVDTQYAQL
TFTDVQEVVD KALANLKQRI EESGAEIEVG SMPAVMADQI QLMQVFQNLI ANGIKFAGDK
SPKIKIWGDR QEDAWVFAVQ DNGIGIDPQF FERIFVIFQR LHTRDEYKGT GMGLAICKKI
IEGHQGQIWL ESNPGEGSTF YFSIPIGN
