SASA_NOSS1
ID SASA_NOSS1 Reviewed; 401 AA.
AC Q8YR50;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Adaptive-response sensory-kinase SasA {ECO:0000255|HAMAP-Rule:MF_01837};
DE EC=2.7.13.3;
GN Name=sasA {ECO:0000255|HAMAP-Rule:MF_01837}; OrderedLocusNames=all3600;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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:0000255|HAMAP-Rule:MF_01837}.
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:0000255|HAMAP-Rule:MF_01837}.
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DR EMBL; BA000019; BAB75299.1; -; Genomic_DNA.
DR PIR; AI2255; AI2255.
DR AlphaFoldDB; Q8YR50; -.
DR SMR; Q8YR50; -.
DR STRING; 103690.17132733; -.
DR EnsemblBacteria; BAB75299; BAB75299; BAB75299.
DR KEGG; ana:all3600; -.
DR eggNOG; COG2205; Bacteria.
DR OMA; AHYGQIW; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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 3: Inferred from homology;
KW ATP-binding; Biological rhythms; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..401
FT /note="Adaptive-response sensory-kinase SasA"
FT /id="PRO_0000074867"
FT DOMAIN 175..400
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
FT MOD_RES 178
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
SQ SEQUENCE 401 AA; 45565 MW; 884243505413FDDC CRC64;
MLKHDSMQVS QDQPIYSEAP LQLLLFVDGR PKSKQQVQRI RAYLKDLQAE YNFELQIIDV
GQQPYLAEHF KLVATPALIK IHPEPRQILA GSNIITQLKN LWPRWQAAAD TYAKLQEDLQ
ERVDDNGRVA QPQSTINSVA VSAELLRLSD EIFNLKQEKE KLLEQLQFKD RVIAMLVHDL
RNPLTAAAIA IETLQSNYNP DIGQFQRLKP ALVVNLLRQA RTQAKTIDKM IADLLQVGRG
TDTELIIIPQ KTEIGLLCLE VLGELRDRYT TKAQKVETDI PQDLPCVYAD PERIRQVLIN
LLDNAIKYTP EGGTISIAGL HRTTQKVQFS IGDTGPGIPS DNRERIFENH YRLERDEAKE
GYGIGLSLCQ RIIRAHYGQI WVDSNPHGGA WFHFTLPVYP S