ID A0A0C2BWI3_9BURK Unreviewed; 605 AA.
AC A0A0C2BWI3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=TSA66_18555 {ECO:0000313|EMBL:KIF82361.1};
OS Noviherbaspirillum autotrophicum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=709839 {ECO:0000313|EMBL:KIF82361.1, ECO:0000313|Proteomes:UP000031572};
RN [1] {ECO:0000313|EMBL:KIF82361.1, ECO:0000313|Proteomes:UP000031572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSA66 {ECO:0000313|EMBL:KIF82361.1,
RC ECO:0000313|Proteomes:UP000031572};
RA Ishii S., Ashida N., Ohno H., Otsuka S., Yokota A., Senoo K.;
RT "Denitrispirillum autotrophicum gen. nov., sp. nov., Denitrifying,
RT Facultatively Autotrophic Bacteria Isolated from Rice Paddy Soil.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC {ECO:0000256|ARBA:ARBA00035100}.
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:KIF82361.1}.
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DR EMBL; JWJG01000028; KIF82361.1; -; Genomic_DNA.
DR RefSeq; WP_040041034.1; NZ_JWJG01000028.1.
DR AlphaFoldDB; A0A0C2BWI3; -.
DR STRING; 709839.TSA66_18555; -.
DR OrthoDB; 9146932at2; -.
DR Proteomes; UP000031572; 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; 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 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; 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 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:UP000031572}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 260..470
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 132..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 605 AA; 63622 MW; FC857DB27FED0BC6 CRC64;
MDDMLKDFVV EALDLATNVE EHLLSLERHP DDTDTLNALF RSFHTIKGGA GFMNLPAIVS
ACHLTENLFD GLRTGKVPVT PTAIEAGLQA SGFVGDQLKQ LANGAAPEAL PAMPEALKDI
LTQAIEGKAT APTAAAPATA PAQSAPDAAT PSASTLPGGD LDWEALYRAV VPAGTLPAPQ
AAAAAPAAPA TVTPIAKAAA EDGAKPVIAQ VKEDTIRIDA IKLDALLEVA GESVQAANQA
AVLLEKLAQF KFEGQAAALM STLAETLARA SRYSTELQRA TLSTRMQPVG RLFQKFPRLV
RELARDLGKD VDLVIEGAET EVDRVVVDSL YDPLVHMLRN ALDHGIETAD ERAATPKAAK
ATIRLKAWQE GSSVMIEVSD DGKGMDPDRL RTKALSKGLI GDNAAQTKEE ALQLIFLPGF
STKEVASSVS GRGVGMDVVK TAVEKHRGAI RIDSELGEGT RFTIRLPIEL SIVPTMLVRT
SGALLAMPMA VVQRVVELPE EFAEVGGAPV LRDQGRPLAV RSLAEILGYE PCREKVGIVI
AAPHPYILAV EGVDGTADLV IKPLTAIAVP GVNGTARSAE GELVLVISLA FLLDGCKILS
NRLAA
//
