ID A0A0P7ZH58_9CYAN Unreviewed; 892 AA.
AC A0A0P7ZH58;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=chpA {ECO:0000313|EMBL:KPQ33961.1};
GN ORFNames=HLUCCO16_17845 {ECO:0000313|EMBL:KPQ33961.1};
OS Phormidium sp. OSCR.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=1666905 {ECO:0000313|EMBL:KPQ33961.1, ECO:0000313|Proteomes:UP000050461};
RN [1] {ECO:0000313|EMBL:KPQ33961.1, ECO:0000313|Proteomes:UP000050461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSCR {ECO:0000313|EMBL:KPQ33961.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPQ33961.1}.
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DR EMBL; LJZT01000096; KPQ33961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7ZH58; -.
DR STRING; 1666905.HLUCCO16_17845; -.
DR PATRIC; fig|1666905.3.peg.3336; -.
DR Proteomes; UP000050461; 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 Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 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; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
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; PF02895; H-kinase_dim; 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 SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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:0000313|EMBL:KPQ33961.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:KPQ33961.1}.
FT DOMAIN 1..109
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 393..602
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 604..746
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 769..886
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 248..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..271
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 819
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 892 AA; 98109 MW; 9A9AE332BDAC3F00 CRC64;
MDDFSALLGT FIAESEEFLR SMETSLLAME TLSATGQKQK QVQQLFRAAH SIKGSASMFG
LTELSAAAHT LEDCFGILRD RADLNQLDPE LINDLLSGVD ILKGLLEKTR TQAAIAPEDY
QDLLPLKQAL EADYQVPESS DEEEEQTSVN SSIVRGIFEM ELPPLLETFE TLISQVNPDN
LSQTQTQLEG LYQQLSGMVQ LLDLPDIAAL IDPLQELVTR ADLSPEELQG QAHPIITALE
QARQQRLGLA SPDPDPQQPT PPQPEPAPTV APSSQRPTIR VDVEALTELV NWVGELVIHR
THLEVQQAQL RSEAKRIRRS VLELNLFGRD LRDEYDRLSV EPHSSASESP NRGFDSLELD
RYSDFHSTAQ SVIETTQAIA QSSGRIDDLS LQLDSNTEQI RRITDRLRSR VYNLRVVPFS
RCVDHLPRAL RELGRQHDKE VNLVLLGRDT QLDESLVDAL RDPLIQLVRN AFDHGIESPQ
ERREAGKPPN GEIEIAASHQ GGQTLITISD DGRGIDANAI RQQAIAQGLI EAEESESLSL
NDIYDFLLLP GFTTSRHPSQ LSGRGVGLDV VTTNLRQVRG TLKVDSQPGK GTRFMIKLPL
MLSITNALLV RVDHQTLAVP LDAVEEILQI DAGQLQMLGN QTMLPWRGEF ICLTRLQDLL
HYNYPTEDEP SPDPLNQDTI PVLVLASAEG VLAIAVERLV GQQEIVVKPI PPPLGKPAGL
VGSTILGDGR VVLIVDTDDL ITQVQPTHSA TPLRVEAHSP GASGTSVRTI LVVDDAYTIR
QLLSLLLQGA NYRVELAKDG QDAFDLLVQG LPCDLVIADI EMPKMDGFEL LEAIKTQPEL
CQIPVAMLTS RSGAKHRQRA LDLGAVDYFT KPYNEAALLG AIAKILTSSP TS
//
