ID A4SKN7_AERS4 Unreviewed; 722 AA.
AC A4SKN7;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:ABO89459.1};
GN OrderedLocusNames=ASA_1357 {ECO:0000313|EMBL:ABO89459.1};
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO89459.1, ECO:0000313|Proteomes:UP000000225};
RN [1] {ECO:0000313|Proteomes:UP000000225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449 {ECO:0000313|Proteomes:UP000000225};
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO89459.1; -; Genomic_DNA.
DR RefSeq; WP_005319290.1; NC_009348.1.
DR AlphaFoldDB; A4SKN7; -.
DR STRING; 29491.GCA_000820065_03205; -.
DR KEGG; asa:ASA_1357; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_7_6; -.
DR Proteomes; UP000000225; Chromosome.
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: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 Kinase {ECO:0000313|EMBL:ABO89459.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:ABO89459.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 372..583
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 585..720
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 263..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 722 AA; 76985 MW; 0508E9FFC75C80E7 CRC64;
MAFEVDEDIL QDFLVEASEI LEQLSEQLVD LEKRPDDKNL LNAIFRGFHT VKGGAGFLSL
GELVDVCHGA ENVFDILRNG KRTVTAELMD VILQALDAIN VMFAQVQNRE PPSPASAEIL
HDLHELCKPE GQEQLLTASA GNNAPAHGEE LVETAVMVSE PETVAAPLPV NGGGSIDEIS
ADEFERLLDE LHGAGGAPTP VANSILTGTG DITDDEFEAL LDQLHGQGQH SGALEVNPLT
SVQKEVDELI DDDEFERLLD ELHGRGQGPK TSITPPAAPV AAAPTPAAPV SAAPAAKPTP
APAPKPAAAP AVAAKPAPAP VKQPSAPAEN AVQSDTTVRV DTKTLDVIMN MVGELVLVRN
RLVSLGIASN DEDMSKAVAN LDVVTADLQG AVMKTRMQPI KKVFGRFPRV VRDLARTLKK
DIELVMVGEE TDLDKNLVEA LADPLVHLVR NSCDHGVEMP DVREKAGKPR QGTITLSASQ
QGDHILLCIE DDGAGMDPEK LKSIAISRGV LDADSAARMS DNDAYNLIFA PGFSTKSEIS
DISGRGVGMD VVKTSIVSLN GSVYIDSTWG KGTRLEIKVP LTLAILPTLM VEVGEQTFAL
PLGCVNEIFH LDLKKANVVD GQLTIIVRDK AIPLFYLHKW LVKGTNKKSR QDTGHVVIVQ
IGTQQIGFVV DNLIGQEEVV IKPLDNLLQG TPGMAGATIT SDGGIALILD VPSLLKAYAR
RH
//
