ID A0A120CU85_HYPSL Unreviewed; 760 AA.
AC A0A120CU85;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=APY04_2696 {ECO:0000313|EMBL:KWT65849.1};
OS Hyphomicrobium sulfonivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT65849.1, ECO:0000313|Proteomes:UP000059074};
RN [1] {ECO:0000313|EMBL:KWT65849.1, ECO:0000313|Proteomes:UP000059074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDL6 {ECO:0000313|EMBL:KWT65849.1,
RC ECO:0000313|Proteomes:UP000059074};
RA Albers P.;
RT "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT consortium.";
RL Submitted (OCT-2015) 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:KWT65849.1}.
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DR EMBL; LMTR01000075; KWT65849.1; -; Genomic_DNA.
DR RefSeq; WP_068463301.1; NZ_LMTR01000075.1.
DR AlphaFoldDB; A0A120CU85; -.
DR STRING; 121290.APY04_2696; -.
DR PATRIC; fig|121290.4.peg.2009; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000059074; 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; cd00731; CheA_reg; 1.
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:SF10; 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 Kinase {ECO:0000313|EMBL:KWT65849.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000059074};
KW Transferase {ECO:0000313|EMBL:KWT65849.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 407..609
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 611..747
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 332..360
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 760 AA; 80559 MW; B42299842CB74555 CRC64;
MDSLRQIFFQ ECEEQLAELE SGLLEIEGGS EDPEIVNAVF RAVHSIKGGA GAFALEDLVR
FAHVFETVLD EVRKGRLSTA SPVTETLLRA ADVLADLVRV ARDGGNVNEE RIHTSADELA
ALSGAPIGAN AEPEEEVSFE DFGFTPVAMD FPVFDGIAVV DTVSVEAEAE PDATTYTITF
RPHPSLYTNA NEPVVLLREL SRLGDAQIVC DTSTIPTLEE LEAEGSYLAW TITLTTTHEE
DDVRSIFEFV DGDCDLEIIT GNAASSNDEP AGVDDDIAAL LARVRGEFTE PVDESASPAA
SAADVVVDLA GSATAETAAA AIPSTPIIEA EAAKPTPEAA KTPPPAKAEK AAGSEAPSTN
QTIRVDLDRV DRLMNLVGEL VINQAMLSQR LTDAGLARDS EFATGLDEFE QLTHDIQEGV
MAIRAQPVKS VFQRMPRLVR EVAAITGKKV RLVTEGEDTE VDKTVIERLA DPLTHMIRNA
IDHGLESPEK RLAAGKREEG LVRLSASHRS GRIVIDIADD GAGINRQRVR AIAEEKGLIQ
PNAQLTDEEV DNLIFLPGFS TASTVSDISG RGVGMDVVKK SIQALGGRVS ITSRPGEGST
FTLSLPLTLA VLYGMVVTVA EQTLVVPLTS IVETLKPKAG DIHGFGGDSR VISMRNNFLP
LIDVGRELGY RSQPADPGAG VALLVESDGG AHSALMVDAI QGQRQIVIKS LEENYGRVPG
VAAATILGDG RVALILDVDA IVAASRSGAS TSETAFALAG
//
