ID A8UVT6_9AQUI Unreviewed; 645 AA.
AC A8UVT6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 08-NOV-2023, entry version 88.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HG1285_00610 {ECO:0000313|EMBL:EDP75220.1};
OS Hydrogenivirga sp. 128-5-R1-1.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX NCBI_TaxID=392423 {ECO:0000313|EMBL:EDP75220.1, ECO:0000313|Proteomes:UP000005981};
RN [1] {ECO:0000313|EMBL:EDP75220.1, ECO:0000313|Proteomes:UP000005981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=128-5-R1-1 {ECO:0000313|EMBL:EDP75220.1,
RC ECO:0000313|Proteomes:UP000005981};
RA Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP75220.1}.
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DR EMBL; ABHJ01000006; EDP75220.1; -; Genomic_DNA.
DR RefSeq; WP_008287290.1; NZ_ABHJ01000006.1.
DR AlphaFoldDB; A8UVT6; -.
DR PATRIC; fig|392423.7.peg.2364; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000005981; 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; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 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; 1.
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; 1.
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; 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.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000005981}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 268..508
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 510..640
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 189..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 645 AA; 71657 MW; C6808D0B4E3A5A36 CRC64;
MISDDMRDIF NEFVVEAEDN LQKVEENLLE LEKDPQNEEL LNATFRAMHT LKGGAGFLGL
NAIVEVAHAA EDVLGKLRSG ELTLTPDIND AILEAVDFIR SALPRYEAGE EVETPQELVK
KLRELEQGGA PSAQEKKEES GIDELLDKYG FGHLKGRPIE DILEELILLP PDERPVELIE
ELDRIVASGE APKAEEKPPE EAPQPEETAI EPAEEVAKEE EVKEEPKEEP RQEQTKAEPK
AEPKKPPIKT EGEKVLRIDV SKIEDLMNLV GELVLERNRL LRVFQKLYEE YQSKTVDEFE
TVMSSLDRIV GDLQLAVMKT RMQPVKRLFQ KFPRVVRDLA RMLGKEVELV LEGEDAEMDK
TVLEKLEEPL IHLIRNAVDH GIEPPDERER LGKPRKGTVK LSAYYHGDRI FIEIADDGRG
IDVEKVKKKA LEKGIISPDR AEKMTEKDIL FLIFHPGFST AEGVSQVSGR GVGMDVVMNT
VSAFRGTIDI DTEQGKGTRI TLSFPLTVGI IRSLLVSVNG RLFAIPIYSV LEIIQGEDAQ
ITTVSGKEVL ILRELTIPLI NLGEALEMGG GNVGYVIVSQ VGSQKVAFTV EDLFGDEEVV
VKPLGKIIGE VQGISGATIT GDGKVVLILD LDGILKREMR TLSLV
//
