ID Q8ECD6_SHEON Unreviewed; 758 AA.
AC Q8ECD6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 136.
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:AAN56206.1};
GN OrderedLocusNames=SO_3207 {ECO:0000313|EMBL:AAN56206.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN56206.1, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN56206.1, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN56206.1,
RC ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN56206.1; -; Genomic_DNA.
DR RefSeq; NP_718762.1; NC_004347.2.
DR RefSeq; WP_011073093.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8ECD6; -.
DR STRING; 211586.SO_3207; -.
DR PaxDb; 211586-SO_3207; -.
DR KEGG; son:SO_3207; -.
DR PATRIC; fig|211586.12.peg.3113; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_6; -.
DR OrthoDB; 9803176at2; -.
DR PhylomeDB; Q8ECD6; -.
DR BioCyc; SONE211586:G1GMP-2987-MONOMER; -.
DR Proteomes; UP000008186; 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:AAN56206.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000008186};
KW Transferase {ECO:0000313|EMBL:AAN56206.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 405..616
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 618..755
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 758 AA; 80821 MW; 968489F630DA2496 CRC64;
MAFDVDEEIL QDFLIEAGEI LELLQEQLVA LENNPDDTDL LNAIFRGFHT VKGGAGFLSL
TPMVDVCHEA ENTFDLLRTG KRSVTAELMD IILQAVDAIN TMFAQTQQGE QQDPADAALL
AKLKLLSSGE PLPSELGQRA PEPELIPEPE PVIETIVEVA VVEEMPVETV DSASSSIDEI
NDAEFEALLD ALHGNGKGPG VATSNVAAAS ISNAVKPPAQ AATSGDDITD DEFEALLDEL
HGSGKFSGKV EESVPAKLKA EVVAAPASAT VPTATSVDSD EITDDEFERL LDELHGKGGT
PVKAVAKAEA AKTVPTPVAA TATPVAPKAS VTAAIPPTVK PKAEVVVAEK APVKAAAAAS
STSVPQGETT VRVDTARLDQ IMNMVGELVL VRNRLVSLGI SRDDEEMSKA LANLDLVTAD
LQGAVMKTRM QPIKKVFGRF PRVVRDLART LNKEIDLVLV GEETDLDKNL VEALADPLVH
LVRNSVDHGI EMPNDREASG KPRTGVITLS ASQEGDHILL KIEDDGAGMD PEKLKQIAIK
RGVLDEDSAA RMTDNEAYNL IFAPGFSTKV EISDISGRGV GMDVVKTRIT QLNGTVHIDS
MKGKGTILEI KVPLTLAIMP TLMVDVAKQV FALPLSSVNE IFHLDLTKTN IVDGQLTVIV
RNKAVPLFYL EHWLHRNKTN FKHGDKKHGH VVIVQLGIMQ IGFVVDALIG QEEVVIKPLG
ALLHGTPGMA GATITSDGGI ALILDVPGLL KHYAKNKS
//
