SASA_SYNE7
ID SASA_SYNE7 Reviewed; 387 AA.
AC Q06904; Q31LC5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Adaptive-response sensory-kinase SasA;
DE EC=2.7.13.3;
DE AltName: Full=Synechococcus adaptive sensor protein A;
GN Name=sasA; Synonyms=sarS; OrderedLocusNames=Synpcc7942_2114;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8370532; DOI=10.1016/0378-1119(93)90679-w;
RA Nagaya M., Aiba H., Mizuno T.;
RT "Cloning of a sensory-kinase-encoding gene that belongs to the two-
RT component regulatory family from the cyanobacterium Synechococcus sp.
RT PCC7942.";
RL Gene 131:119-124(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH KAIC, AND MUTAGENESIS OF HIS-161.
RX PubMed=10786837; DOI=10.1016/s0092-8674(00)80832-6;
RA Iwasaki H., Williams S.B., Kitayama Y., Ishiura M., Golden S.S., Kondo T.;
RT "A kaiC-interacting sensory histidine kinase, SasA, necessary to sustain
RT robust circadian oscillation in cyanobacteria.";
RL Cell 101:223-233(2000).
RN [4]
RP STRUCTURE BY NMR OF 4-103.
RX PubMed=15313603; DOI=10.1016/j.jmb.2004.07.010;
RA Vakonakis I., Klewer D.A., Williams S.B., Golden S.S., LiWang A.C.;
RT "Structure of the N-terminal domain of the circadian clock-associated
RT histidine kinase SasA.";
RL J. Mol. Biol. 342:9-17(2004).
CC -!- FUNCTION: May be involved in signal transduction. Participates in the
CC KaiABC clock protein complex, which constitutes the main circadian
CC regulator in cyanobacteria, via its interaction with KaiC. Required for
CC robustness of the circadian rhythm of gene expression and is involved
CC in clock outputs. {ECO:0000269|PubMed:10786837}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Interacts with KaiC. Participates in the KaiABC complex, whose
CC core is composed of a KaiC homohexamer, a KaiB dimer and two KaiA
CC dimers. {ECO:0000269|PubMed:10786837}.
CC -!- INTERACTION:
CC Q06904; Q79PF4: kaiC; NbExp=6; IntAct=EBI-626872, EBI-592287;
CC -!- DOMAIN: Although the N-terminal domain, which mediates the interaction
CC with KaiC, shares some sequence similarity with KaiB, it is not
CC structurally related to KaiB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D14056; BAA03145.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58144.1; -; Genomic_DNA.
DR PIR; JN0793; JN0793.
DR RefSeq; WP_011378322.1; NC_007604.1.
DR PDB; 1T4Y; NMR; -; A=4-103.
DR PDB; 1T4Z; NMR; -; A=4-103.
DR PDBsum; 1T4Y; -.
DR PDBsum; 1T4Z; -.
DR AlphaFoldDB; Q06904; -.
DR BMRB; Q06904; -.
DR SMR; Q06904; -.
DR IntAct; Q06904; 3.
DR STRING; 1140.Synpcc7942_2114; -.
DR PRIDE; Q06904; -.
DR EnsemblBacteria; ABB58144; ABB58144; Synpcc7942_2114.
DR KEGG; syf:Synpcc7942_2114; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_723030_0_0_3; -.
DR OMA; AHYGQIW; -.
DR OrthoDB; 1755994at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2114-MON; -.
DR EvolutionaryTrace; Q06904; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IMP:CACAO.
DR GO; GO:0007623; P:circadian rhythm; IEA:UniProtKB-UniRule.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd02978; KaiB_like; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_01837; Kinase_SasA; 1.
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; IPR011649; KaiB_domain.
DR InterPro; IPR023527; Kinase_SasA.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF07689; KaiB; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM01248; KaiB; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biological rhythms; Kinase; Nucleotide-binding;
KW Phosphoprotein; Transferase; Two-component regulatory system.
FT CHAIN 1..387
FT /note="Adaptive-response sensory-kinase SasA"
FT /id="PRO_0000074872"
FT DOMAIN 158..382
FT /note="Histidine kinase"
FT REGION 1..97
FT /note="Interaction with KaiC"
FT MOD_RES 161
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MUTAGEN 161
FT /note="H->Q: Lowers the amplitude of circadian rhythm."
FT /evidence="ECO:0000269|PubMed:10786837"
FT CONFLICT 135
FT /note="F -> L (in Ref. 1; BAA03145)"
FT /evidence="ECO:0000305"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1T4Y"
FT HELIX 24..40
FT /evidence="ECO:0007829|PDB:1T4Y"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1T4Y"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1T4Y"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1T4Y"
FT STRAND 67..78
FT /evidence="ECO:0007829|PDB:1T4Y"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1T4Y"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:1T4Y"
SQ SEQUENCE 387 AA; 43315 MW; 04A0A097C3EE0438 CRC64;
MGESLSPQAL AQPLLLQLFV DTRPLSQHIV QRVKNILAAV EATVPISLQV INVADQPQLV
EYYRLVVTPA LVKIGPGSRQ VLSGIDLTDQ LANQLPQWLV QQEAFFADRE PPEVNIPFTE
LGQPETPALQ QADAFFQLQQ QYADLSERTK FLEQVIALVA HDLRNPLTAA LLAVDTIQIR
SQSFSVATAK EMQGLCSLFD QARSQLREIE RMIAEILEAT RHSGESLRIN PREVVFEPLL
QQVLEQLHER WRSKQQQLIT DVPGDLPTLY ADPDRLRQVL VNLLDNAIKY TPPGGTITIA
ALHRTSQKVQ ISISDTGSGI PRDQLSVIFK NLVRLSRDSS QEGYGIGLSV CQRIVQAHFG
RIWVASELGQ GSTFHFTMPV YRYTMPC
