ID A0A431VC40_9PROT Unreviewed; 947 AA.
AC A0A431VC40;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EJ903_21070 {ECO:0000313|EMBL:RTR16280.1};
OS Azospirillum griseum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2496639 {ECO:0000313|EMBL:RTR16280.1, ECO:0000313|Proteomes:UP000277007};
RN [1] {ECO:0000313|EMBL:RTR16280.1, ECO:0000313|Proteomes:UP000277007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-25-5w-1 {ECO:0000313|EMBL:RTR16280.1,
RC ECO:0000313|Proteomes:UP000277007};
RA Yang Y.;
RL Submitted (DEC-2018) 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:RTR16280.1}.
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DR EMBL; RXMA01000026; RTR16280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A431VC40; -.
DR OrthoDB; 7292702at2; -.
DR Proteomes; UP000277007; 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; 2.40.50.180; CheA-289, Domain 4; 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; 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; 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; PS50851; CHEW; 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:UP000277007}.
FT DOMAIN 4..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 545..785
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 787..923
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 459..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 947 AA; 99318 MW; 454DA1272338DFC4 CRC64;
MSGPDDPIEE FWSLFGAELD EYLAAIEGIL AASPVDPARV DELFRAFHSV KGGSAALALR
CIETVAHAAE DVLHLVRAGK RALDTDLVSA LLEAVDEMRR LQDTAMATRT DQPVNAAIVA
RLKDHLTGGA PAASPVAPAV PAALPMVEPV AVPAAERPSA LIVDPPVLER MQDAVLGLIG
AIDAEDPGEA ALALVEAAEP ADLHGVVGAA FRLAGGGAGR WGWLDLVLRL RAVESASGES
VGAFALSAAL ETLFADLLLE QAGSLKSTPE DPAVWLHAAR LFVGLEVDAG AELADLIAAR
LLRGEQTPDV DELADLCALT GIAASSGMEI PRDEITALRD RWLGAEGVVA EEAPVVPSTE
HAHAWPADTR MRMAVAEADG SALLLVLLDL ERDPAVAESV TEALRAERSL YNRSRLDLRG
GMFEYVVAVR GDAAVFARSL TDLDPGRACV RSIRRTDANA APGAELADTT AQPLPTQSPP
AQPSSTPARE AQAAASVAPP APLPPTLSPP TLSPVAAPAG AGGGAPRPVD AMVRVPSAAI
DGFMDLIGEL RLGLTALSLT LGEEGTRPTN PKARATHDGM RRLDRAVRQL YEGALGLRVV
PIGTLFSRLL RPIRDTAVLV GKEVGLTTAG EDVQVDKAMI EMLVDPLTHI VRNSVDHGIE
SPERRAAAGK PAQGSIRIRA RQTASLAIVE VEDDGGGIDV ARVRDKAVSK GLIGAADAAA
LPDAEALNLI LLPGFSTRDE VTATSGRGVG MDIVLTAIKK LGGTLAIDSH PGQGTRMTIE
FPVSAAMQRV LTAEVAGQLV AIHERSVREV VDVTPDRLRR IGRRLSLSLR GRFLPVVDLG
ALLGLRPPSP DDPTTRRTVV VVDDGDAQIG LMIDRMAVRR EVFFKRLHPL IEDNTLIAGA
AVIGAGSVMF ALDTPTLFAR AVTWLDPNPH SNPDGRSGDK EDPCSAD
//
