ID KAIB_SYNE7 Reviewed; 102 AA. AC Q79PF5; Q31NX2; Q9Z3H3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 116. DE RecName: Full=Circadian clock oscillator protein KaiB {ECO:0000255|HAMAP-Rule:MF_01835, ECO:0000303|PubMed:9727980}; GN Name=kaiB {ECO:0000255|HAMAP-Rule:MF_01835, ECO:0000303|PubMed:9727980}; GN OrderedLocusNames=Synpcc7942_1217; ORFNames=see0010; OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) OS (Anacystis nidulans R2). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=1140; RN [1] {ECO:0000312|EMBL:BAA37102.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DISRUPTION RP PHENOTYPE, AND MUTAGENESIS OF LEU-11 AND ARG-74. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=9727980; DOI=10.1126/science.281.5382.1519; RA Ishiura M., Kutsuna S., Aoki S., Iwasaki H., Andersson C.R., Tanabe A., RA Golden S.S., Johnson C.H., Kondo T.; RT "Expression of a gene cluster kaiABC as a circadian feedback process in RT cyanobacteria."; RL Science 281:1519-1523(1998). RN [2] {ECO:0000312|EMBL:AAM82685.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RA Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., McMurtry S., RA Gonzalez A., Salinas I., Golden S.S., Youderian P.; RT "Synechococcus elongatus PCC7942 cosmid 7G3."; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000312|EMBL:ABB57247.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33912 / 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 [4] RP HOMODIMERIZATION, AND INTERACTION WITH KAIA AND KAIC. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=10064581; DOI=10.1093/emboj/18.5.1137; RA Iwasaki H., Taniguchi Y., Ishiura M., Kondo T.; RT "Physical interactions among circadian clock proteins KaiA, KaiB and KaiC RT in cyanobacteria."; RL EMBO J. 18:1137-1145(1999). RN [5] RP FUNCTION, AND INTERACTION WITH KAIC. RX PubMed=12727878; DOI=10.1093/emboj/cdg168; RA Xu Y., Mori T., Johnson C.H.; RT "Cyanobacterial circadian clockwork: roles of KaiA, KaiB and the kaiBC RT promoter in regulating KaiC."; RL EMBO J. 22:2117-2126(2003). RN [6] RP FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND INTERACTION WITH RP KAIC. RX PubMed=12727879; DOI=10.1093/emboj/cdg212; RA Kitayama Y., Iwasaki H., Nishiwaki T., Kondo T.; RT "KaiB functions as an attenuator of KaiC phosphorylation in the RT cyanobacterial circadian clock system."; RL EMBO J. 22:2127-2134(2003). RN [7] RP FUNCTION OF THE KAIABC COMPLEX, AND INDUCTION. RX PubMed=14709675; DOI=10.1073/pnas.0307411100; RA Nakahira Y., Katayama M., Miyashita H., Kutsuna S., Iwasaki H., Oyama T., RA Kondo T.; RT "Global gene repression by KaiC as a master process of prokaryotic RT circadian system."; RL Proc. Natl. Acad. Sci. U.S.A. 101:881-885(2004). RN [8] RP INTERACTION WITH KAIC. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; 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 [9] RP SUBUNIT. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=15347812; DOI=10.1073/pnas.0403906101; RA Nishiwaki T., Satomi Y., Nakajima M., Lee C., Kiyohara R., Kageyama H., RA Kitayama Y., Temamoto M., Yamaguchi A., Hijikata A., Go M., Iwasaki H., RA Takao T., Kondo T.; RT "Role of KaiC phosphorylation in the circadian clock system of RT Synechococcus elongatus PCC 7942."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13927-13932(2004). RN [10] RP FUNCTION, AND RECONSTITUTION OF KAIABC OSCILLATOR. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=15831759; DOI=10.1126/science.1108451; RA Nakajima M., Imai K., Ito H., Nishiwaki T., Murayama Y., Iwasaki H., RA Oyama T., Kondo T.; RT "Reconstitution of circadian oscillation of cyanobacterial KaiC RT phosphorylation in vitro."; RL Science 308:414-415(2005). RN [11] RP FUNCTION, DOMAIN, AND MUTAGENESIS OF 95-GLU--ASP-101 AND 95-GLU--GLU-108. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=16227211; DOI=10.1074/jbc.m503360200; RA Iwase R., Imada K., Hayashi F., Uzumaki T., Morishita M., Onai K., RA Furukawa Y., Namba K., Ishiura M.; RT "Functionally important substructures of circadian clock protein KaiB in a RT unique tetramer complex."; RL J. Biol. Chem. 280:43141-43149(2005). RN [12] RP FUNCTION, INTERACTION WITH KAIC, AND SUBUNIT. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=17717528; DOI=10.1038/sj.emboj.7601832; RA Nishiwaki T., Satomi Y., Kitayama Y., Terauchi K., Kiyohara R., Takao T., RA Kondo T.; RT "A sequential program of dual phosphorylation of KaiC as a basis for RT circadian rhythm in cyanobacteria."; RL EMBO J. 26:4029-4037(2007). RN [13] RP FUNCTION. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=17916691; DOI=10.1126/science.1148596; RA Rust M.J., Markson J.S., Lane W.S., Fisher D.S., O'Shea E.K.; RT "Ordered phosphorylation governs oscillation of a three-protein circadian RT clock."; RL Science 318:809-812(2007). RN [14] RP SUBUNIT, AND INTERACTION WITH KAIC. RX PubMed=24474762; DOI=10.1073/pnas.1314326111; RA Snijder J., Burnley R.J., Wiegard A., Melquiond A.S., Bonvin A.M., RA Axmann I.M., Heck A.J.; RT "Insight into cyanobacterial circadian timing from structural details of RT the KaiB-KaiC interaction."; RL Proc. Natl. Acad. Sci. U.S.A. 111:1379-1384(2014). RN [15] RP FUNCTION, SUBUNIT, FOLD-SWITCH, DOMAIN, DISRUPTION PHENOTYPE, AND RP MUTAGENESIS OF 88-GLY--ASP-90 AND GLY-88. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=26113641; DOI=10.1126/science.1260031; RA Chang Y.G., Cohen S.E., Phong C., Myers W.K., Kim Y.I., Tseng R., Lin J., RA Zhang L., Boyd J.S., Lee Y., Kang S., Lee D., Li S., Britt R.D., Rust M.J., RA Golden S.S., LiWang A.; RT "Circadian rhythms. A protein fold switch joins the circadian oscillator to RT clock output in cyanobacteria."; RL Science 349:324-328(2015). RN [16] RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ALA-40 AND RP LYS-42. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=28302851; DOI=10.1126/science.aag2516; RA Tseng R., Goularte N.F., Chavan A., Luu J., Cohen S.E., Chang Y.G., RA Heisler J., Li S., Michael A.K., Tripathi S., Golden S.S., LiWang A., RA Partch C.L.; RT "Structural basis of the day-night transition in a bacterial circadian RT clock."; RL Science 355:1174-1180(2017). RN [17] RP SUBUNIT. RX PubMed=29892030; DOI=10.1038/s41598-018-27131-8; RA Mukaiyama A., Furuike Y., Abe J., Koda S.I., Yamashita E., Kondo T., RA Akiyama S.; RT "Conformational rearrangements of the C1 ring in KaiC measure the timing of RT assembly with KaiB."; RL Sci. Rep. 8:8803-8803(2018). RN [18] RP CLOCK RECONSTITUTION, FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-22. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=34618577; DOI=10.1126/science.abd4453; RA Chavan A.G., Swan J.A., Heisler J., Sancar C., Ernst D.C., Fang M., RA Palacios J.G., Spangler R.K., Bagshaw C.R., Tripathi S., Crosby P., RA Golden S.S., Partch C.L., LiWang A.; RT "Reconstitution of an intact clock reveals mechanisms of circadian RT timekeeping."; RL Science 374:eabd4453-eabd4453(2021). RN [19] {ECO:0007744|PDB:4KSO} RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS), STRUCTURE BY CRYO-ELECTRON RP MICROSCOPY (16.0 ANGSTROMS) IN COMPLEX WITH KAIC, AND SUBUNIT. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RX PubMed=23796516; DOI=10.1016/j.jmb.2013.06.018; RA Villarreal S.A., Pattanayek R., Williams D.R., Mori T., Qin X., RA Johnson C.H., Egli M., Stewart P.L.; RT "CryoEM and molecular dynamics of the circadian KaiB-KaiC complex indicates RT that KaiB monomers interact with KaiC and block ATP binding clefts."; RL J. Mol. Biol. 425:3311-3324(2013). RN [20] {ECO:0007744|PDB:5N8Y} RP STRUCTURE BY ELECTRON MICROSCOPY (4.70 ANGSTROMS) OF OSCILLATOR COMPLEXES, RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF LYS-42. RX PubMed=28302852; DOI=10.1126/science.aag3218; RA Snijder J., Schuller J.M., Wiegard A., Lossl P., Schmelling N., RA Axmann I.M., Plitzko J.M., Forster F., Heck A.J.; RT "Structures of the cyanobacterial circadian oscillator frozen in a fully RT assembled state."; RL Science 355:1181-1184(2017). CC -!- FUNCTION: Key component of the KaiABC oscillator complex, which CC constitutes the main circadian regulator in cyanobacteria CC (PubMed:28302852, PubMed:9727980, PubMed:17717528). Complex composition CC changes during the circadian cycle to control KaiC phosphorylation. CC KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, CC leading to KaiC autodephosphorylation. KaiA binding to the KaiC CII CC domain yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC CC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding CC of KaiB to form the KaiB(6):KaiC(6) complex, leading to changes in the CC output regulators CikA and SasA. KaiB switches to a thioredoxin-like CC fold (KaiB(fs)) in complex with KaiC (PubMed:28302852, PubMed:26113641, CC PubMed:28302851). KaiB(6):KaiC(6) formation exposes a site for KaiA CC binding that sequesters KaiA from the CII domain, making the CC KaiC(6):KaiB(6):KaiA(12) complex that results in KaiC CC autodephosphorylation (PubMed:17717528, PubMed:17916691, CC PubMed:28302852). Complete dephosphorylation of KaiC leads to CC dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai CC oscillator (PubMed:28302852). {ECO:0000269|PubMed:12727878, CC ECO:0000269|PubMed:12727879, ECO:0000269|PubMed:14709675, CC ECO:0000269|PubMed:17717528, ECO:0000269|PubMed:17916691, CC ECO:0000269|PubMed:26113641, ECO:0000269|PubMed:28302851, CC ECO:0000269|PubMed:28302852, ECO:0000269|PubMed:9727980}. CC -!- FUNCTION: Circadian oscillations can be generated in vitro by CC incubating KaiA, KaiB and KaiC with 1 mM ATP. The cycle is self- CC sustainable for at least 3 cycles and resistant to temperature changes CC (PubMed:15831759). A very robust clock is reconstituted with KaiA, CC KaiB, KaiC, SasA, CikA and RpaA; output is measured by transcription CC from an appropriate reporter (PubMed:34618577). CC {ECO:0000269|PubMed:15831759, ECO:0000269|PubMed:34618577}. CC -!- FUNCTION: A metamorphic protein which reversibly switches between an CC inactive tetrameric fold and a rare, thioredoxin-like monomeric fold CC (KaiB(fs)). KaiB(fs) binds phospho-KaiC, KaiA and CikA. KaiA and CikA CC compete for binding to KaiB(fs), and KaiB(fs) and SasA compete for CC binding to KaiC, thus the clock oscillator and output signal pathway CC are tightly coupled. {ECO:0000255|HAMAP-Rule:MF_01835, CC ECO:0000269|PubMed:26113641, ECO:0000269|PubMed:28302851}. CC -!- SUBUNIT: Undergoes a major conformational rearrangment; in the free CC state forms homotetramers with 2 dimers (PubMed:23796516). When bound CC to the CI domain of KaiC switches to a monomeric thioredoxin-fold CC (KaiB(fs)) (PubMed:26113641, PubMed:28302851, PubMed:28302852). CC Monomers, homodimers and homotetramers are detected in solution; at low CC concentrations only monomers are seen. In vitro forms KaiC(6):KaiB(1) CC and KaiC(6):KaiB(6) complexes (PubMed:24474762). Only associates with CC 'Ser-431'-phosphorylated KaiC (and not with doubly phosphorylated KaiC) CC (PubMed:17717528, PubMed:29892030). Complex formation between KaiB and CC KaiC is regulated by the phosphorylation state of KaiC and by an ATP CC hydrolysis-driven conformation change in the CI ring of KaiC; complex CC formation is slow. Slow complex formation is crucial for the timing of CC the circadian period (PubMed:29892030). In low resolution cryo-EM forms CC a KaiC(6):KaiB(6) complex (PubMed:23796516). The KaiABC complex CC composition changes during the circadian cycle to control KaiC CC phosphorylation. Complexes KaiC(6), KaiA(2-4):KaiC(6), KaiB(6):KaiC(6) CC and KaiC(6):KaiB(6):KaiA(12) are among the most important forms, many CC form cooperatively (PubMed:28302852, PubMed:34618577). The KaiB:KaiC CC complex is more prevalent at 16 hours (in the dark) than at 4 hours (in CC the light) in the circadian cycle (PubMed:10786837). The KaiA:KaiB CC complex is only found at 20-24 hours in the circadian cycle (subjective CC night) (PubMed:15347812). Binds to the CI domain of KaiC; SasA and KaiB CC compete to bind to the CI domain (PubMed:26113641, PubMed:28302851, CC PubMed:28302852). {ECO:0000269|PubMed:10064581, CC ECO:0000269|PubMed:10786837, ECO:0000269|PubMed:12727878, CC ECO:0000269|PubMed:12727879, ECO:0000269|PubMed:15347812, CC ECO:0000269|PubMed:17717528, ECO:0000269|PubMed:23796516, CC ECO:0000269|PubMed:24474762, ECO:0000269|PubMed:26113641, CC ECO:0000269|PubMed:28302851, ECO:0000269|PubMed:28302852, CC ECO:0000269|PubMed:29892030, ECO:0000269|PubMed:34618577, CC ECO:0000312|PDB:4KSO, ECO:0000312|PDB:5N8Y}. CC -!- INTERACTION: CC Q79PF5; Q79PF6: kaiA; NbExp=11; IntAct=EBI-619150, EBI-592281; CC Q79PF5; Q79PF5: kaiB; NbExp=5; IntAct=EBI-619150, EBI-619150; CC Q79PF5; Q79PF4: kaiC; NbExp=12; IntAct=EBI-619150, EBI-592287; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12727879}. Cell CC membrane {ECO:0000269|PubMed:12727879}; Peripheral membrane protein CC {ECO:0000269|PubMed:12727879}. Note=From circadian time (CT) 12-16 to CC CT 20 the major fraction is membrane-associated, is then translocated CC to the cytosol, where it probably interacts with KaiC and KaiA. CC -!- DEVELOPMENTAL STAGE: Accumulates in a circadian fashion, peaking at CT CC 15-18. {ECO:0000269|PubMed:12727879}. CC -!- INDUCTION: Transcribed in a circadian rhythm with maximal expression at CC 12 hours and minimal expression 12 hours later; expressed as a kaiB- CC kaiC opperon (PubMed:9727980). Down-regulated by KaiC (PubMed:9727980, CC PubMed:14709675). {ECO:0000269|PubMed:14709675, CC ECO:0000269|PubMed:9727980}. CC -!- DOMAIN: The C-terminal region may confer species specificity; C- CC terminal hybrids do not all rescue deletions in S.elongatus PCC 7942 CC (PubMed:16227211). Has 2 forms, fold switches to a thioredoxin-like CC fold (KaiB(fs)) when bound to KaiC (PubMed:28302852, PubMed:26113641). CC The KaiB(fs) form binds faster to KaiC than wild-type, thus less fully CC phosphorylated KaiC forms; the KaiB(fs) form activates signaling CC through CikA and inhibits signaling through SasA (PubMed:26113641) CC (Probable). A mutant locked in the KaiB(fs) form binds the CikA PsR CC domain (PubMed:26113641). {ECO:0000269|PubMed:16227211, CC ECO:0000269|PubMed:26113641, ECO:0000269|PubMed:28302852, CC ECO:0000305|PubMed:26113641}. CC -!- DISRUPTION PHENOTYPE: Not essential for growth on low light, loss of CC circadian cycle and rhythmicity (PubMed:9727980). Cells elongate CC (PubMed:26113641, PubMed:28302851). {ECO:0000269|PubMed:26113641, CC ECO:0000269|PubMed:28302851, ECO:0000269|PubMed:9727980}. CC -!- MISCELLANEOUS: 'Kai' means 'cycle' in Japanese. CC {ECO:0000303|PubMed:9727980}. CC -!- SIMILARITY: Belongs to the KaiB family. {ECO:0000255|HAMAP- CC Rule:MF_01835, ECO:0000305}. 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; AB010691; BAA37102.1; -; Genomic_DNA. DR EMBL; AY120853; AAM82685.1; -; Genomic_DNA. DR EMBL; CP000100; ABB57247.1; -; Genomic_DNA. DR PIR; T44268; T44268. DR RefSeq; WP_011242647.1; NZ_JACJTX010000003.1. DR PDB; 4KSO; X-ray; 2.62 A; A/B/C/D=1-102. DR PDB; 5N8Y; EM; 4.70 A; G/H/I/J/K/L=1-102. DR PDBsum; 4KSO; -. DR PDBsum; 5N8Y; -. DR AlphaFoldDB; Q79PF5; -. DR EMDB; EMD-3602; -. DR EMDB; EMD-5672; -. DR SASBDB; Q79PF5; -. DR SMR; Q79PF5; -. DR DIP; DIP-33331N; -. DR IntAct; Q79PF5; 2. DR STRING; 1140.Synpcc7942_1217; -. DR PaxDb; 1140-Synpcc7942_1217; -. DR GeneID; 76399958; -. DR KEGG; syf:Synpcc7942_1217; -. DR eggNOG; COG4251; Bacteria. DR HOGENOM; CLU_144073_0_0_3; -. DR OMA; NEFKGVY; -. DR OrthoDB; 5458519at2; -. DR BioCyc; SYNEL:SYNPCC7942_1217-MONOMER; -. DR Proteomes; UP000889800; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0007623; P:circadian rhythm; IEA:UniProtKB-UniRule. DR GO; GO:0009649; P:entrainment of circadian clock; IDA:UniProtKB. DR GO; GO:0042326; P:negative regulation of phosphorylation; IDA:CACAO. DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:CACAO. DR CDD; cd02978; KaiB_like; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR HAMAP; MF_01835; KaiB; 1. DR InterPro; IPR013474; Circ_KaiB. DR InterPro; IPR039022; KaiB-like. DR InterPro; IPR011649; KaiB_domain. DR InterPro; IPR036249; Thioredoxin-like_sf. DR NCBIfam; TIGR02654; circ_KaiB; 1. DR PANTHER; PTHR41709; KAIB-LIKE PROTEIN 1; 1. DR PANTHER; PTHR41709:SF2; KAIB-LIKE PROTEIN 1; 1. DR Pfam; PF07689; KaiB; 1. DR SMART; SM01248; KaiB; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Biological rhythms; Cell membrane; Cytoplasm; Membrane; KW Reference proteome. FT CHAIN 1..102 FT /note="Circadian clock oscillator protein KaiB" FT /id="PRO_0000217767" FT MUTAGEN 11 FT /note="L->F: In kaiB1; shortens the period of the circadian FT rhythm to 21 hours." FT /evidence="ECO:0000269|PubMed:9727980" FT MUTAGEN 22 FT /note="R->A: Decrease in cooperativity of KaiB(fs) FT recruitment." FT /evidence="ECO:0000269|PubMed:34618577" FT MUTAGEN 40 FT /note="A->D: Disrupts circadian rhythms in vivo, cells FT elongate." FT /evidence="ECO:0000269|PubMed:28302851" FT MUTAGEN 42 FT /note="K->A: Loss of KaiA binding." FT /evidence="ECO:0000269|PubMed:28302852" FT MUTAGEN 42 FT /note="K->E: Disrupts circadian rhythms in vivo." FT /evidence="ECO:0000269|PubMed:28302851" FT MUTAGEN 74 FT /note="R->W: In kaiB2; shortens the period of the circadian FT rhythm to 22 hours." FT /evidence="ECO:0000269|PubMed:9727980" FT MUTAGEN 88..90 FT /note="GLD->ALR: Stabilizes the KaiB(fs) form, disrupts FT KaiC phosphorylation rhythms, does not form a complex with FT KaiA, dominant-negative over wild-type protein, restores FT normal cell-length to disruption strains, disturbs FT regulation of SasA and CikA. Binds CikA PsR." FT /evidence="ECO:0000269|PubMed:26113641" FT MUTAGEN 88 FT /note="G->A: Stabilizes the KaiB(fs) form, disrupts KaiC FT phosphorylation rhythms, forms a complex with KaiA, wild- FT type regulation of SasA, disturbs regulation of CikA, FT dominant-negative over wild-type protein, restores normal FT cell-length to disruption strains (i.e. contributes to SasA FT and CikA regulation)." FT /evidence="ECO:0000269|PubMed:26113641" FT MUTAGEN 95..102 FT /note="Missing: Circadian rhythm strongly weakened and FT destabilized." FT /evidence="ECO:0000269|PubMed:16227211" FT MUTAGEN 95..101 FT /note="ELQDSDD->QELQNNSN: Circadian rhythm strongly FT weakened and destabilized." FT /evidence="ECO:0000269|PubMed:16227211" FT STRAND 7..15 FT /evidence="ECO:0007829|PDB:4KSO" FT HELIX 18..33 FT /evidence="ECO:0007829|PDB:4KSO" FT TURN 36..38 FT /evidence="ECO:0007829|PDB:4KSO" FT STRAND 39..45 FT /evidence="ECO:0007829|PDB:4KSO" FT TURN 46..48 FT /evidence="ECO:0007829|PDB:4KSO" FT HELIX 61..64 FT /evidence="ECO:0007829|PDB:4KSO" FT HELIX 70..81 FT /evidence="ECO:0007829|PDB:4KSO" FT STRAND 86..92 FT /evidence="ECO:0007829|PDB:4KSO" SQ SEQUENCE 102 AA; 11436 MW; 4E7FD086742A398F CRC64; MSPRKTYILK LYVAGNTPNS VRALKTLKNI LEVEFQGVYA LKVIDVLKNP QLAEEDKILA TPTLAKVLPL PVRRIIGDLS DREKVLIGLD LLYGELQDSD DF //