ID A0A239DBM1_9SPHN Unreviewed; 817 AA.
AC A0A239DBM1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN06295955_101178 {ECO:0000313|EMBL:SNS29458.1};
OS Sphingopyxis indica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=436663 {ECO:0000313|EMBL:SNS29458.1, ECO:0000313|Proteomes:UP000198339};
RN [1] {ECO:0000313|EMBL:SNS29458.1, ECO:0000313|Proteomes:UP000198339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS15 {ECO:0000313|EMBL:SNS29458.1,
RC ECO:0000313|Proteomes:UP000198339};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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};
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DR EMBL; FZPA01000001; SNS29458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239DBM1; -.
DR Proteomes; UP000198339; 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; 3.30.565.10; 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; 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; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SNS29458.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000198339};
KW Transferase {ECO:0000313|EMBL:SNS29458.1}.
FT DOMAIN 12..116
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 166..417
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 419..557
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 59
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 817 AA; 86788 MW; 0D3F34DE2A8DA7D7 CRC64;
MFAMVAARLG APVTAMDDLL NDFLAETSEI LAEAGGALVA WEADPADRER LDAIFRFVHT
IKGSSGFLSL PRVTALAHAA EDALDQVRRG QRQADAALVT AVLGIVDRLS DLCAALGTQG
SEPAGDDSAV IAALASTGSA PVAPAESAAE PARSDAEADD LSVDLQAWRS IRVPLPLLDS
VMTGVTDIVL ARNEFSRMLR ESGADASLVA SFDRLSDSIA AMRQSVSHMR MQRIDKLFAP
LPRIVRDLAQ DLGKKVEFSA TGGEVELDRE MMENIRDPLI HIVRNALDHG IEPLDQRVAA
GKSVTATLSV SARQSGNQIE IEVRDDGRGL SPDALAAKAI ASRILTAAEA RALSPKDKLE
LIFRPGFSTA AKVTSVSGRG VGMDIVKANL ERIGGIVELR NEEGRGLAIV LRVPMTLTII
SGLMVRAAAQ YFAIPRGAVR EILLENSDSV RIDRVGGGEL VTVRGEQFPL LRLETILDCD
VDESDDADER AIVIVRPGQG LSYAISVAAI HDHEELVIKP AAPPIMATGL YAGTTLPDNG
RPVLLLDVQG VMAAAAIDAS ESGRAAAGAG EAEDAAASVR DAAQLLLFRD IDQRLRGVRL
SVIERVEEVP VLALFESAGQ VRAQIGEQIF PVHADRLPDT QGTVKLLRLH DGRAVLCYPI
DAVIDIVRLP DAVQPAATPG LIAGVVLVGG EPVEVIDPFW LMERYAPVAA SLVETRQPLC
TLAGDQDGWG DNFLAPLLRQ AGYRVAGSDE AGGERPDVML CLADDPAQCG VAGDDVPMIR
LRASLEAAAS DEESVYRYDR QALLEALRRR VGGGRAA
//
