ID A0A563W4L4_9CYAN Unreviewed; 1030 AA.
AC A0A563W4L4;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 08-OCT-2025, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=H1P_820014 {ECO:0000313|EMBL:VEP18587.1};
OS Hyella patelloides LEGE 07179.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
OC Hyellaceae; Hyella.
OX NCBI_TaxID=945734 {ECO:0000313|EMBL:VEP18587.1, ECO:0000313|Proteomes:UP000320055};
RN [1] {ECO:0000313|EMBL:VEP18587.1, ECO:0000313|Proteomes:UP000320055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1 {ECO:0000313|EMBL:VEP18587.1};
RA Brito A.;
RL Submitted (JAN-2019) 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};
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DR EMBL; CAACVJ010000690; VEP18587.1; -; Genomic_DNA.
DR RefSeq; WP_144867961.1; NZ_LR213840.1.
DR AlphaFoldDB; A0A563W4L4; -.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000320055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR051315; Bact_Chemotaxis_CheA.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR003594; HATPase_dom.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:VEP18587.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000320055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..107
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 499..733
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 735..879
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 911..1028
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 462..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 961
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1030 AA; 113728 MW; DFCD3C3961AEC88F CRC64;
MSDDKELQVR LQFLEEAGEY LDNIESGLLG LGSNQVNPQQ MDGVLRAAHS IKGGAAMMGF
ESLSHLAHRL EDFFKILKVG KSKAVDSSLE TLLLSTVDFL RQIIVVNRQQ QQVNSQWLKT
TVETVFKQLH DRLGDPQPED AAALLSAEMG EDMSTLIFET EVEELLSQLE NKLEKLEPHS
LLEELKLSAQ ELGGLGEILE LPAFFSLCQS VIDLVESSPE KVNSIAQTAI QEWRRSQALV
LIGQTEVLPE TLELDEDDVF FSDSSLDADA LIEELPDSTD LASLLGGDEL EQEALDIFSS
LDEMIPEELS TAELEAIDLS ALDLEEIDMD IPAAVPVAEF SVEEITPEYS ISAEPDNSVA
NYPTPSISPT TFSTTSSGEM AANDDNAVVN KTIRVSVKQL EYLSDLFGEV AIERNGLGLR
LTSLRNLVNL LSQRIKTLEQ SNFSLRIAYD KVATETVTTR PSESIAVNSA SHSLQPSAEN
SSEEYFDSLE MDSYSDIHLL SQEVMETVVQ IQEVTKDIEI NLEDTEKNSR ELNRTTKHMQ
STLTKVRMRP LSDLLNRFPR ALRDLELQYG KKAQLRVRGA STLVERSIVE ILNDPLLHLF
RNAFDHGIEP PAIRKAAGKS EQGTITITAS HRGNQTVITM GDDGEGINLE KIKTKALSMG
VSREDLVNAK EADLLDLIFE PGFSTAQAVT DLSGRGVGMD VVKTNIEEIN GKIQVNTELG
VGTTFTITVP FTLSVVRVLL VESNGMLLAF PTSIVEEMLV LDPDTILEAA GQEVLNWDGF
IVRLIRLHQW LNLPDFASGS PVELEETPTI EQSTVLMIAQ NNDLVGIQVD RYWREQEVTI
RSVEGKMALP PGFTGCTVLG NGRVVPLVDA ISLLSWIEND RQASATSSYS LKIGNSDSSE
KPGKPAATKK TIMVVDDSIN VRRFLALTLE KANYRVEQAK DGQDAIDKLQ AGVSPQAVIC
DIEMPRLDGF GFLSRVRTLR QHKNLPVIML TSRSGDKHRK LAMSLGATEY FSKPFKENTL
LSTLKKLILR
//
