ID K7YT33_BDEBC Unreviewed; 682 AA.
AC K7YT33;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:AFY03056.1};
GN ORFNames=Bdt_3381 {ECO:0000313|EMBL:AFY03056.1};
OS Bdellovibrio bacteriovorus str. Tiberius.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=1069642 {ECO:0000313|EMBL:AFY03056.1, ECO:0000313|Proteomes:UP000010074};
RN [1] {ECO:0000313|EMBL:AFY03056.1, ECO:0000313|Proteomes:UP000010074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tiberius {ECO:0000313|EMBL:AFY03056.1,
RC ECO:0000313|Proteomes:UP000010074};
RX PubMed=23181807; DOI=10.1186/1471-2164-13-670;
RA Hobley L., Lerner T.R., Williams L.E., Lambert C., Till R., Milner D.S.,
RA Basford S.M., Capeness M.J., Fenton A.K., Atterbury R.J., Harris M.A.,
RA Sockett R.E.;
RT "Genome analysis of a simultaneously predatory and prey-independent, novel
RT Bdellovibrio bacteriovorus from the River Tiber, supports in silico
RT predictions of both ancient and recent lateral gene transfer from diverse
RT bacteria.";
RL BMC Genomics 13:670-670(2012).
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; CP002930; AFY03056.1; -; Genomic_DNA.
DR RefSeq; WP_015092465.1; NC_019567.1.
DR AlphaFoldDB; K7YT33; -.
DR STRING; 1069642.Bdt_3381; -.
DR KEGG; bbat:Bdt_3381; -.
DR PATRIC; fig|1069642.3.peg.3348; -.
DR HOGENOM; CLU_000650_3_7_7; -.
DR Proteomes; UP000010074; 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; 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}.
FT DOMAIN 4..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 317..523
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 525..676
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 51
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 682 AA; 72812 MW; 047C61D6ED1D1DC4 CRC64;
MSGDNSFFEE LQMDFLNESA FMLEQYEEYM MRLENSEDPA KDLTDIFRVA HSVKGGAAAV
GLADLCKFAH VMEDLLDLLR SRPELVNSTV ISLLLQSGDE LKNRVAALQQ QQGGPWDPSA
LTAELIAITE QLSGKASKHA HAPAPSVDEP KVEVPDDFFS QAPAAEASAG AEDDLINHDL
LAELLAQMSP EDQAEFHAKE AAEAALKTAI AESAPVAAEP ANPAPILKVV ETPMEAPASA
VKAAPAAAAK PAAAASAAGN GGGNNKNAKN ATSAIKVDTG RVDSVLDAVG ELVVLKNQLV
HDETVRSGVN LRLEAIVDQL DKAVRELYEK TLSIRMTPLK SMFIKIQRIV RDVSLTLDKP
VDLQLIGEET EVERTVFELL GDPLVHLVRN SMDHGVEKKE LRQERGKPAT AKVTVSAKQS
GGNVIIDISD DGGGINRDKV LGKAIEKGFV PAGVDPASIP DEQVFQYIFY PGFSTADKIS
DLSGRGVGLD VVKSNLDKIN GKINIYSKSG QGTTFRLTIP LSTAITDGII VALDGARYIL
PIHSIREIVR VLPKDYTNIS GAGKVASIRG HLLPVIDVSK TLGSINWSLN KKDQQLAQRR
ENSLSARREE TMLVIIESMT GQMAFPVDDV LGQAQVVVKP ITTGQDIPEV AGAAILGDGR
TVLILEPGAL VNNIANGRGM AA
//
