ID A0A1F6PHD5_9BACT Unreviewed; 1119 AA.
AC A0A1F6PHD5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2039_06525 {ECO:0000313|EMBL:OGH95586.1};
OS Candidatus Melainabacteria bacterium GWA2_34_9.
OC Bacteria; Candidatus Melainabacteria.
OX NCBI_TaxID=1801604 {ECO:0000313|EMBL:OGH95586.1, ECO:0000313|Proteomes:UP000198266};
RN [1] {ECO:0000313|EMBL:OGH95586.1, ECO:0000313|Proteomes:UP000198266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGH95586.1}.
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DR EMBL; MFRJ01000110; OGH95586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6PHD5; -.
DR STRING; 1801604.A2039_06525; -.
DR Proteomes; UP000198266; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 4..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 627..841
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 843..977
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1001..1117
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 133..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..36
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 502..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1050
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1119 AA; 126714 MW; D876D189D8F10F54 CRC64;
MDFLESEIVE ILNIFREESE EQLQKLNKNL LKLEANPKDN TAISELFREA HSLKGAARMI
GLNDIQLIAH KLEDVFGMAK ECRLNVTPET IDILCKAIDC INSIVEESIE TRGNASFDNV
PEMVQKLENI INSENSEPDD ENNSNQEKNS SLESDQRLNN RKSDWQQNLN YFDINKINKE
NKTLIIQTKV NIEKIKIFSS SSDAIEELLH FIIRLKSAII ALDNQRLTGI IEDIKIKLEA
ALKGSGILTS DEVWEIEENF ETFSSLFDRL TAVQETKNDP IPQPDNMNIL NETPLFNPEP
APYSEESIQQ HIDTAKESTQ SEETISQDSN PLSNFILEGN IDDDLKNNIL NASLENKNQK
EDLIFIKNNI TIFSIHSQEN ILKFDEVIKK LNNFLKTIED ESIKNIIEKL TELLTYSKEK
NTPISTDVVQ IIKESFEAAV LMINSPFEVQ DNPVLILQRL AVLYQMIKLS DTEQYIIEEE
TKESNEENSS KLSTLKTGTE ILSKNTPTSE NDNSAFEMKP GDSNTIKTLR VDTKKLDQLV
SQVGELIIAK IKAKDHLSEL EKIIRSVEEW HREWNKTKQY FKHIDKPHYK SIDLPAGSSI
YSQNKNLSVF FEENSAKLSG LTNKMNQLYK IIHEDDTRLH LIVNELEERI KSVRVLPLAT
IFHMFPRMVR DIAREKNKNI ELIISGSETS VDKKIIEEIK SPLIHIIRNS IDHGIEDTQT
RIKNGKNPVG KIFLAAYHLE NSVLIEIIDD GHGINIEAIK RKVLQKQLLA QEELDSMTEE
QIMNIIFWPG FSTGETVTDI SGRGIGLDIV YTKISQLNGK VKIKSTLGEG CRVSIQLPVT
MATIKSFLVE VNNQKFAIPT STIKTTLLIS PENIFYKEGK KTIIVEDATV PICNLCDTLD
LAENNHKNKK LVVIVVQSED IQVGFIVDKL VGDQEILHKN LSPPLLRVRN IAGVTTLGSG
ELCLILNIGD LVKTAYSKFG VVEKRMITDK NPEQNITSEK RILVVDDSLT TRILERNILK
AAGYNVTVAV NGLEALTKLA TEDYDIVITD VEMPEINGFE LTERLREQEK FKNMPIILVT
SLSSEIDKRK GIGLGANAYL TKGNFNQDEL LANVRKLLS
//
