SASA_THEVB
ID SASA_THEVB Reviewed; 380 AA.
AC Q8DMT2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=tlr0029;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC07582.1; -; Genomic_DNA.
DR RefSeq; NP_680820.1; NC_004113.1.
DR RefSeq; WP_011055884.1; NC_004113.1.
DR PDB; 6X61; X-ray; 3.20 A; B/D/F/H/J/L=16-107.
DR PDBsum; 6X61; -.
DR AlphaFoldDB; Q8DMT2; -.
DR SMR; Q8DMT2; -.
DR STRING; 197221.22293750; -.
DR EnsemblBacteria; BAC07582; BAC07582; BAC07582.
DR KEGG; tel:tlr0029; -.
DR PATRIC; fig|197221.4.peg.28; -.
DR eggNOG; COG2205; Bacteria.
DR OMA; AHYGQIW; -.
DR OrthoDB; 1755994at2; -.
DR Proteomes; UP000000440; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biological rhythms; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..380
FT /note="Adaptive-response sensory-kinase SasA"
FT /id="PRO_0000074871"
FT DOMAIN 157..380
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
FT MOD_RES 160
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:6X61"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:6X61"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6X61"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6X61"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:6X61"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:6X61"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6X61"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:6X61"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:6X61"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:6X61"
SQ SEQUENCE 380 AA; 43266 MW; 80A205ABEB612E01 CRC64;
MKASADASSP QETTPPLSLL LFVANRPGDE EETAAIQAHI QQLPSNFSFE LKVVPIGEQP
YLLEEYKLVA TPALIKVRPE PRQTLAGRKL LQKVDYWWPR WQREVALGLQ ADMQKSAAEQ
SDCSMELSRL KDELFQLRQE RDRLAEQLQF KDRIISLLAH ELRNPLTAGG IALETLESNL
QEESSQQLPI EDIQRLFHHA RSQTQTMGQL ITDLLLAARG PQDKLQIMAR QLDLRQLCQE
TVEDVRLNFE RKKQHFTTDI PLDLPLVYGD GDRIRQVLVN LLDNACKYTP EGGKIHLSAF
HRMTQKVQVT VSDTGPGIPI EQQEKIFGET VRLDRDRAIE GYGIGLALCR QIIRMHYGQI
WVDSQPGKGS CFHFTLPVYS
