ID A0A3N1HQS8_9ACTN Unreviewed; 772 AA.
AC A0A3N1HQS8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EDC03_1008 {ECO:0000313|EMBL:ROP44878.1};
OS Pseudokineococcus lusitanus.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Pseudokineococcus.
OX NCBI_TaxID=763993 {ECO:0000313|EMBL:ROP44878.1, ECO:0000313|Proteomes:UP000276232};
RN [1] {ECO:0000313|EMBL:ROP44878.1, ECO:0000313|Proteomes:UP000276232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7306 {ECO:0000313|EMBL:ROP44878.1,
RC ECO:0000313|Proteomes:UP000276232};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
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:ROP44878.1}.
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DR EMBL; RJKN01000002; ROP44878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1HQS8; -.
DR InParanoid; A0A3N1HQS8; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000276232; 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 Gene3D; 2.40.50.180; CheA-289, Domain 4; 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; 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 PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 2.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 2.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 2.
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; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ROP44878.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000276232};
KW Transferase {ECO:0000313|EMBL:ROP44878.1}.
FT DOMAIN 11..121
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 193..437
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 439..586
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 602..744
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 153..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..766
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 772 AA; 79073 MW; 59E524B6ABD17373 CRC64;
MGGGPGGTGE ADDGLDELVR DFLLETEEGL VDVDRALVAL EADPTSSRAP ALLAAVFRTV
HTVKGTCGFL DLPRLEELAH AGETLLVPLR DGARVLEPAT TDVLLHLVDG LRAVLAVVAA
TGSDAGADTA GLLAEVAACA AAGAEEASAA PAAAQPVRAA GPGPAPAPVP APRPPAAPAP
ATADVRGAEQ SVRVDVEVLE ELVALVGELV LTRNQVVERA ARSGDAEVVR AAHRLDVVAG
SLQRSVMQTR MQPMEHAWAS LPRVVRDLGH QLGRQVRLVT EGGGTELDRS LLEAVKDPLL
HLVRNAVDHG LEAPEGRRAA GKHPTGTLTL RARHESGQVV VEVVDDGRGM DPATIAARAY
ERGVADEATL RRMSTGELLA LVFTPGFSTA TEVTAVSGRG VGMDVVRTNV ERIGGSVELD
SVPGRGTTTR LRVPLTLAIV PALLVGCAGD RYALPQGALR ELVALTPGRT APGGVVAGAV
SGTAERVGGV EVMRLRGRLL PLVRLRAELG LPPAAPGEGA VVAVLETAGR RFGLVVDAVH
ASQEIVVKPL GRHLRAVPAY AGATILGDGG LALILDVPSL ARSTREGDRP ALEAPEAAPV
VRVPLLLVDV GRHRVGIPLP AVARLDEVAD RALERLGTRW AARRRGEVLT VVDLADHLAR
AAGEARAPRR PGSASGRPAV PLVVLDAPDG DPVGLVVGSV LDVVEVPAEE VRPATDGGLV
GVAEVGGRLV GVLDAAAVLA ATARPPVPGV EVPRPRPAPS APATTTAPGG PA
//
