ID A0A0D8ZWR9_9CYAN Unreviewed; 884 AA.
AC A0A0D8ZWR9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 08-OCT-2025, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=UH38_03870 {ECO:0000313|EMBL:KJH73195.1};
OS Aliterella atlantica CENA595.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Aliterellaceae; Aliterella.
OX NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH73195.1, ECO:0000313|Proteomes:UP000032452};
RN [1] {ECO:0000313|EMBL:KJH73195.1, ECO:0000313|Proteomes:UP000032452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA595 {ECO:0000313|EMBL:KJH73195.1,
RC ECO:0000313|Proteomes:UP000032452};
RA Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P.,
RA Fiore M.F.;
RT "Draft genome of a novel marine cyanobacterium (Chroococcales) isolated
RT from South Atlantic Ocean.";
RL Submitted (FEB-2015) 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 -!- 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:KJH73195.1}.
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DR EMBL; JYON01000002; KJH73195.1; -; Genomic_DNA.
DR RefSeq; WP_045053297.1; NZ_CAWMDP010000059.1.
DR AlphaFoldDB; A0A0D8ZWR9; -.
DR STRING; 1618023.UH38_03870; -.
DR PATRIC; fig|1618023.3.peg.5265; -.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000032452; 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; 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000032452};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 361..597
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 599..740
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 763..880
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 376..410
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 813
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 884 AA; 98416 MW; C245BFCECC6B5AF2 CRC64;
MSDDTENEIR LQFLEEAQEY AKTIEAKLIE LASNKSDRID AILRAAHSIK GGAAMMGFQK
LSDLAHRLED FFKVLKIQPD LIDRDLEQLL LAAVDCLQQV ISYNLQGMIV DEQWLASQAY
PLFDQLDRLI GSPQAEDERN IGGEDGQDMA ALIFETEVED YLQRLESLLV NPQENDLLPE
ISSMAQDLGS FGEMLQLNAF AKLCASISQQ LADTPEQVVS IAEQALQAWR RSQAIILVGE
IQALPTSLNL DAEAQEPDSE LFLADFDLTN LDAEVEQLAS SAKTLSLPGA NNSAEAQEYQ
ESTVRVPTKL LERLNDWFGE LTIARNGINI YVERLHSLNK LLERRVQAVE KERIMPVGEL
PTTQSVEASE AMLQALVQLQ EVKDDIELTL EESDRAVSDL NRVAKQLQTS LTQVRMRPFA
DLVARFPRFI RELCLEYGKN AQLKVIGEQT LIERTILEAL NNPLMHLLRN AFDHGIEPVE
IRQASGKPEV GLIEIKAVYQ GNQTLITVKD DGGGINLEQI RTKAQQLGID SNISDEKLLS
LIFEPGFSTA NQVTALSGRG VGMDIVRTNL RQIRGDIKVD TQLGVGTTFT LSVPFTLSVM
RVIAIEINSL LLAFPSEAIR EVLLFSASQF CEIAGNEAIS WEGRIAPLIR LEEWLKVRHL
PQKAAESKLL APEPTVLTIE RENEWVGLLV ERSWKEQEVA IRQVEPGIEM PTGFSSCAIL
GDGRVAPLVD VPQLLDWINN FGQSGDRPLE TPTRETEGEA KDTILVVDDS INVRRFLSLT
LEKAGYRVEQ AQDGLSALEK LSAELPIKAV ICDLDMPNLD GFGLLARVKS NPAFARLPIA
MLTSRSGQKD RQTAMQLGAT AYFAKPYNEH ELLQTLKQML HKRS
//
