ID A0A926T767_9CYAN Unreviewed; 1417 AA.
AC A0A926T767;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
DE RecName: Full=Circadian input-output histidine kinase CikA {ECO:0000256|ARBA:ARBA00074306};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=H6F73_14910 {ECO:0000313|EMBL:MBD1938593.1};
OS Microcoleus sp. FACHB-68.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Microcoleus.
OX NCBI_TaxID=2692826 {ECO:0000313|EMBL:MBD1938593.1, ECO:0000313|Proteomes:UP000627787};
RN [1] {ECO:0000313|EMBL:MBD1938593.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-68 {ECO:0000313|EMBL:MBD1938593.1};
RX PubMed=32943748;
RA Chen M.Y., Teng W.K., Zhao L., Hu C.X., Zhou Y.K., Han B.P., Song L.R.,
RA Shu W.S.;
RT "Comparative genomics reveals insights into cyanobacterial evolution and
RT habitat adaptation.";
RL ISME J. 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:MBD1938593.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-68 {ECO:0000313|EMBL:MBD1938593.1};
RA Chen M., Teng W., Zhao L., Hu C., Zhou Y., Han B., Song L., Shu W.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBD1938593.1}.
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DR EMBL; JACJOT010000008; MBD1938593.1; -; Genomic_DNA.
DR RefSeq; WP_190759444.1; NZ_JACJOT010000008.1.
DR Proteomes; UP000627787; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR FunFam; 3.30.565.10:FF:000010; Sensor histidine kinase RcsC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR050903; Bact_Chemotaxis_MeTrfase.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF27; PROTEIN-GLUTAMATE O-METHYLTRANSFERASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000627787};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 30..209
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 225..521
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 1033..1257
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1292..1414
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 694..767
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1345
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1417 AA; 157995 MW; DEA9A981ACA84862 CRC64;
MNPIESSSQS ENQATAAGTA DENQQNENQL FPIVGIGASA GGLEAFTALL KALPTDTGMA
FVLIQHLAPQ HKSLLTEILS KTTQMPVKEV EEGMIVEPNS VYIIPPNTKM AIVRGELKLM
PREKIEGKYM PVDAFLQSLS MDRKNKAIGV VLSGMDGDGT LGVEAIKSEG GITFAQCEDT
AKYDSMPNNA VASGRVDFIL PPKEIALKLG NISRHPYVTQ PIPLSANDLL FENPNLLQQI
FSLLLASAGV DFTCYKHPTI KRRIMRRMAL YQFPTLEDYV AYLQETPDEV TALYKDILIN
FTCFFRDPES FEVLKNKVFP SIIKDKPLDT PIRIWVPGCS TGEEVYSIAI CLQEFLEAEE
TNIPIQIFAT DISDSAIEKA RAGIYTDKQV QDVSPASLQQ FFIKLNESGY QIKKYIRDKC
IFAKQNVSQD PPFSKLDLIS CRNMLIYLGP ALQKKIIPLF HYALNPIGFL MLGSSETTGE
FSDLFALVDK KQKIYSRKFA PTRQNFNFAT TTYPVEKLTT NKPIDEEIPK TLDLQKEADR
IVLSKYAPAG VVINDEMDIL QFRGDISLYL EPAPGTASLN LLKMLRTVFL LAVRTAIHQA
KEQNIPIKKE GIQVKNQEQS REVNIEVIPF KPDTSVEVYF LVLFEDVTPI SSESKVTKFS
WINALKGNQK TDQTAQDREI VRLLQELTAT KEYLQSIIAE KEASNEELII ANEEILSSNE
EFQSTNEELQ TAKEEIQATN EELNTINEEL KNRNVEISQV NNDLSNLLNS VNIPILMLGK
DLCIRLFTPL AKTVLNIIST DVGRSIGDIQ THINVPHLEK LIREVIDTGT IAELEIQERS
GYWYNLRILP YLTRDNKIDG AVLVLVDIDA LKHSAQQLQE SRDYAEAIVA TVRAPLVVLD
SQLRVKTVNR SFYETFQVTP EETEQKLIFD LGNGQWNIPR LRQLLEQVLS QDTLIHDFEV
THEFLNIGNK TMLLNACRIP LDGNPMQMML LGIEDITERK QFEDERNRLF VCEQSARESA
ETANRAKDEF LSLLSHELRN PLSAILGWSK LLRTRNLDEI QTSRGLEVIE RSVQAQNRLI
EDMLDITRIT TGKLRLNVVP VSLPSVIERA ISIVRLSAEA KNIQLESVIN FPTLKMVGDP
DRLQQIMWNL LSNAIKFSRD GGRIEVKLEK IKDEPADCFY AQIAVSDTGM GIAPEFLPFV
FERFRQADNT SVKSSGGLGL GLALVRHLVE LHGGTVHAES AGEGLGSTFI VRLPVQNVCE
LDRTFANYSP QLKLTNDTEA MLDDAPNLEG LHILVVDDEV DTQELLAAIL QLCGAEVTAV
GSAGAAMSVL MGNSLYGQPA VLVSDISMPE EDGYALMDQV RALEASQGGA IPAVALTANA
GVEDRIRVLQ SGFQIHISKP VEPAELVFVV AKLAQRI
//
