ID A0A075WSJ2_9BACT Unreviewed; 898 AA.
AC A0A075WSJ2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 08-NOV-2023, entry version 49.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HL41_02985 {ECO:0000313|EMBL:AIH03836.1};
OS Thermodesulfobacterium commune DSM 2178.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=289377 {ECO:0000313|EMBL:AIH03836.1, ECO:0000313|Proteomes:UP000028481};
RN [1] {ECO:0000313|EMBL:AIH03836.1, ECO:0000313|Proteomes:UP000028481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2178 {ECO:0000313|EMBL:AIH03836.1,
RC ECO:0000313|Proteomes:UP000028481};
RX PubMed=25635017;
RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA Robb F.T., Ward N.L., Eisen J.A.;
RT "Genome Sequence of a Sulfate-Reducing Thermophilic Bacterium,
RT Thermodesulfobacterium commune DSM 2178T (Phylum Thermodesulfobacteria).";
RL Genome Announc. 3:0-0(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};
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DR EMBL; CP008796; AIH03836.1; -; Genomic_DNA.
DR RefSeq; WP_028841746.1; NZ_JQLF01000015.1.
DR AlphaFoldDB; A0A075WSJ2; -.
DR STRING; 289377.HL41_02985; -.
DR PaxDb; 289377-HL41_02985; -.
DR KEGG; tcm:HL41_02985; -.
DR eggNOG; COG0643; Bacteria.
DR HOGENOM; CLU_000650_5_2_0; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000028481; Chromosome.
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; 3.40.50.2300; -; 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; 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; 2.
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; 2.
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; 2.
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; 2.
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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000028481}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 259..475
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 477..611
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 634..765
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 781..898
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 134..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..39
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 134..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 831
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 898 AA; 101489 MW; 6401FFB09566D007 CRC64;
MMFDEDILQD FLVEAKEAIA NLEEGFLELE KDKENLEVIR SLFRSMHSLK GASGFFGFKS
LESIAHFSEE ILSKIRDGLL KPDDSIIDML LKAVDWIKFI VQHLETHKEE PIDDNLLEFL
VTLSNFTEKI KKGIKEEKSS EKPIEEPVQE ISEKISQGTQ QETSQETQQE PLQVPSEEAI
PKKTLEESVE KEEKKEEKTQ KMVEKLDDKK EKKESPQVAT PQVELTETHI KVDVKLLDQL
MNLAGELVLA RNRVVQLSQK ILDDDLTRSV QALSMITTEM QETIMKTRMQ PIGTVFNKFP
RIVRDLAKSL GKKVNLHLEG TETELDRSII EAIKDPLTHL VRNAIDHGIE PPEERVQVGK
REEGTIYLRA YQEGGQVVIE IEDDGRGIDV EKIRKKAVEK GFLTAEEAQR ARESDLLALI
FKPGFSTAEK VTQVSGRGVG MDVVKTNIEK LGGTIEINTI YGKGTTVRVK IPLTLAIIPA
LIVKSGGYKY AIPQVNLKEL VNVDPNKDLL KVGSTDFYRL RGEIIPVLKL SEILKQSSNG
EVLSKNLVIL TTGERVLGLL VDEILNSEEI VVKPLGKWFK DIPVYSGATI MGDGALALIL
DVVGLSKFIG LSVEEVEKRL DAERITIKTS KDETYFLLLF DVGQDRLALP IALISRLDKV
KADSIQIVGG KEVIIYEDQV VPVIRLENYL PLQGLPYQDS YIVLFFTERS KTCAILCSSI
VDTIETTLEI EEGLYNNPGI LGHKIIDGKT VLFIDIYKVI EMYDPEWFVV KFKEEVHTAK
RILLAEDSPF FRNMMKNYLE AMGFEVECVE NGREAIEKLH NDPNFDLVIT DIEMPEMDGF
ELLKELRGNP QFKNLPVIVV TALAGEEVKR KVFEFGANGY EVKLQRDQVL ERIKQLLS
//
