ID A0A1H7HDB3_9GAMM Unreviewed; 709 AA.
AC A0A1H7HDB3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216262_101465 {ECO:0000313|EMBL:SEK48284.1};
OS Colwellia chukchiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=641665 {ECO:0000313|EMBL:SEK48284.1, ECO:0000313|Proteomes:UP000199297};
RN [1] {ECO:0000313|Proteomes:UP000199297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9127 {ECO:0000313|Proteomes:UP000199297};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOBI01000001; SEK48284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7HDB3; -.
DR STRING; 641665.GCA_002104455_00240; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000199297; 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: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:SEK48284.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000199297};
KW Transferase {ECO:0000313|EMBL:SEK48284.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 347..563
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 565..699
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 127..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 709 AA; 76036 MW; 82D059E7731F0E6A CRC64;
MSFEQDEEIL QDFLIEAGEI LETLSEQLVE LENDPDNADL LNAIFRGFHT VKGGAGFLSL
TELVDACHGA ENVFDTLRNQ QRAVTSSLMD VILQALDTIN EMFAQVQNRA PLSSADPALL
AELHRLSEPE GQESSSPEQP PAQQGVAPKP DVNLEENNAD DEMSEDEFER LLDELHGGGA
PSASVSTPPA PSASPAADAN NNDISDDEFE SLLDELHGQG TFSPAVATSH NAPAPASSSD
EINDDEFEAL LDELHGKGQG PKVAPVSEPA KATPTPAAAP VTAVTPAKAV KPAPKPATVS
NDGAAAPAAK APQAETTVRV DTKRLDQIMN MVGELVLVRN RLTSLGMTKE DEELTKAVSN
LDAVTTDLQG AVMKTRMQPI KKVFGRFPRV VRDLARSLNK EIKLILEGED TDLDKNLVEA
LADPLVHLVR NSVDHGIEDP DTREAAGKAR EGVVVLSASQ EGDHILLTIR DDGAGMNAEK
LKAIAIERGV LDADAAARMP DKEAFSLIFA PGFSTKTEIS EVSGRGVGMD VVKTKITQLN
GTVSIDSEMG VGTILEIKVP LTLAILPTLM VMIGKQTFAL PLATVNEIFH LDLTKTNLVD
GQLTIIVREK AIPLFYLDQW LAKDYQDKPR DRGHVVIVQL GNQQIGFVVD SLIGQEEVVI
KPLDRLLHGT PGMAGATITS DGGIALIIDV PSMLKYYAKK SIVNKKLRS
//
