ID V4RN09_9CAUL Unreviewed; 872 AA.
AC V4RN09;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ABENE_07360 {ECO:0000313|EMBL:ESQ92628.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ92628.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ92628.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ92628.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ92628.1}.
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DR EMBL; AWGB01000011; ESQ92628.1; -; Genomic_DNA.
DR RefSeq; WP_018082529.1; NZ_AWGB01000011.1.
DR AlphaFoldDB; V4RN09; -.
DR STRING; 1121022.GCA_000376105_02862; -.
DR PATRIC; fig|1121022.4.peg.1473; -.
DR eggNOG; COG0643; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000017837; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000017837}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 538..741
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 743..872
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 446..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 872 AA; 94274 MW; 1E0B3740A1246754 CRC64;
MKSLLARFIP EARDLIESSS SGLLKLEKTP NDISVVNEVF RAVHTLKGSS GLFDVPALTR
LVHVAEDLLG AVRAEELNID PQLVDHLLST LDQVGVWINH LETEATLPED ADRISQSMST
VLKQAFSKSG ETAVDGKSGA DAEPEFRRLA ASALDGCDPD DRFEAFAQLV SGLSVQCVEY
QPADDCFFNG TDPLAMMLSL PGLISLTAFP VASFAAITEL DPYRCNLRFQ ALSVAPKSDI
EHHLRYELDH VVLTEVYAED LIVVSGLPSD LAVFGDFYNE AVELLARDAF AQIARSAKAL
GAVTGPDLAS TKALLWLASA LEASTPDKSL VAALIEAVLT GTFRRPQVHA TPAVPSALRR
PFKRALDIIS SQMRGLQEIP FEPSVLTGPK ATVSNLLRSL DRDELLDSVE TAGEQCVEAG
SFDPFLHLLE KLVADIPSFA GAENGAPSLS KAAVEQPLKV DEADKGSAQD ERDASIRADP
KQAPSRILKV DQGKIDALMN LIGELVVSKN SLPFLARRAE EVHGSREMSR EIKEQYAIID
RLAQEMQAAI MQVRMLPIAD VFDRFPRLVR DLSRKLAKDI SLVIEGGDTA ADKNIIEALN
DPLLHIVRNS LDHGVEPPAE RVAAGKPQCA TIGLKAYQEA DYVVIEVNDD GRGMDPAKIR
ASAVKKGVIT PDEAGRLSDQ EAINLIFRPG FSTAEKISDL SGRGVGMDVV RTAIEKLGGR
VSVTSRIGEG SNTKLMLPLS MAVTRVMIIE AASDLFGVPM DLIVETVRVE TKRIHKIKQA
EAFVLRDQLI PLVRMADLLS LPARPLVDDA EAVLVCRIDG RLVGLVIDDF RVGMDVIVKP
LEGIVAGIPG FSGTTLLGDG RVLLVLDLKE LV
//
