ID L8MY81_9CYAN Unreviewed; 573 AA.
AC L8MY81;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Pse7429DRAFT_3458 {ECO:0000313|EMBL:ELS31420.1};
OS Pseudanabaena biceps PCC 7429.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=927668 {ECO:0000313|EMBL:ELS31420.1, ECO:0000313|Proteomes:UP000011201};
RN [1] {ECO:0000313|EMBL:ELS31420.1, ECO:0000313|Proteomes:UP000011201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7429 {ECO:0000313|EMBL:ELS31420.1,
RC ECO:0000313|Proteomes:UP000011201};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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 -!- 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:ELS31420.1}.
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DR EMBL; ALWB01000173; ELS31420.1; -; Genomic_DNA.
DR RefSeq; WP_009628493.1; NZ_ALWB01000173.1.
DR AlphaFoldDB; L8MY81; -.
DR PATRIC; fig|927668.3.peg.3927; -.
DR OrthoDB; 415285at2; -.
DR Proteomes; UP000011201; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13431; TPR_17; 1.
DR Pfam; PF14559; TPR_19; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00386; HAT; 3.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELS31420.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:ELS31420.1}.
FT REPEAT 65..98
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 343..569
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 573 AA; 65459 MW; 323F2BE2347AD21E CRC64;
MHFILELAQQ GQFQRASELF EQCLELDPNN FRTLNSYANA LVQQGEYLHA SELFEHSLKS
NKSNVPTLNS YANALVEQGE YQRASELFEQ CLELDPNNFR TLNSYADVLA RQGQYKRAVE
VQPYYSYALL KYAQQLEARG DIQEALTQLS VIDLSSQKTY HANIIRLCLG RLYYRLGQID
LGKQFFDEAI ANSEDQDKST LYAARSLLAT NPNSQEAINL LLKIQEDSPR YADAMKAIAL
NADAETSYEL FGADEEQIDD IEMLYRAMYH KIGNEIAVLR SISYRLLKRM EGEHPLVKEI
VNDFEKLQQG IASQRANEKA AIAQVSHSNY KQLIEIVSKT AHDISDEVNN QLAVIESKTR
RAMRKLTAGN PQYQQFEKLL VQLKITQKAI NDLKSINEGK TIRRNRFLVH RLFEKWEPEN
WTSQPRIDGV RIRLDIRNPD SEFNGDEEKI KSILNELVEN SLKHNYGNSN LSIRMYSSDL
LNPSDISSPT IPGDRKFLYI EFTDNGQGVP SDKKDWIFQP LKTTSPEDKG SGLGLFIARK
TIKKMGGQIR EVGEAGKGVR FQIYLPYLSA NIL
//
