ID I3YDV8_THIV6 Unreviewed; 1872 AA.
AC I3YDV8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Thivi_3303 {ECO:0000313|EMBL:AFL75176.1};
OS Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS violascens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocystis.
OX NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL75176.1, ECO:0000313|Proteomes:UP000006062};
RN [1] {ECO:0000313|EMBL:AFL75176.1, ECO:0000313|Proteomes:UP000006062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17096 / DSM 198 / 6111
RC {ECO:0000313|Proteomes:UP000006062};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of Thiocystis violascens DSM 198.";
RL Submitted (JUN-2012) 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; CP003154; AFL75176.1; -; Genomic_DNA.
DR RefSeq; WP_014779583.1; NC_018012.1.
DR STRING; 765911.Thivi_3303; -.
DR KEGG; tvi:Thivi_3303; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_0_1_6; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000006062; 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; cd00088; HPT; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 3.
DR Pfam; PF00072; Response_reg; 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; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 4.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFL75176.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000006062};
KW Transferase {ECO:0000313|EMBL:AFL75176.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 621..725
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 783..885
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1060..1164
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1360..1593
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1595..1733
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1751..1867
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1217..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 668
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 828
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1107
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1800
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1872 AA; 201910 MW; F4FA49AA9F969AA3 CRC64;
MAEKKVVEGL KWVKGEIAAT LRPVRALVEA DGVSAVPQDP TAAVQALEQV HGVLLALQLK
APARLAREMT LLAERMRDGL AGEDPADARS GTRAMGQALA QLNHHLDRLD AGFDESPRSL
WPIIDAVRAA CDVQPLTHAE QLSFAAADTN GASPGTPETL ENLAEVVRQV RPQYHRYLVE
WYRGDPNRQS LPRLGGLFHH LHDSLREGVL ADLFRLAEVF TEALRNGALA TDARARSLMG
HLDRVLKALS QQPPQWPEVD ALSLIDHLLR SLSEGGVNSP LIAQLQSLYD SSQSVTALPR
ADLEGLGGDE ALAELARALL SEFAQLKEQF DRLARDAQTD RTALDAFCAH LRRLADTLDV
AEVGNLPNRL RALATDFGAL ALDEIAEDQA RLESHAMELL GIEAVLLAHA DHRSTRPRQL
IAPDMDLSEL TAATLREAGY ELVRVKDAIA NCHVDQGIRE TLNPVRQHLF SVSGALNILG
EIPAARLAES IGELVQQRYV KAEHAPTDAE FEHLADAVAA LELYIGHLQD AVPFGDSLIE
RGGQSIRALQ SEPGDTLAPP IGEIANALSV SIDLDLDLDL DEALPLDATA PPDVPASGQE
QPISDHGISE ALPGLIESEF SDDDETEFLD IFMEEAREET ASAQIQFARW ESNPNDTAAL
ASLRRSFHTL KGSGRLVGAL QVAEFGQAVE FLLNRLIEDQ ALPSEEILAC VAEAVNLLPE
LVTAESEGRP FDIDPLISRA NRLRESANLV PGPEPMIDPG QPLSLDAPAG EALADQVTDH
DSLFVADEEL LRIFQAETHE HLAELRAFLR RAEAGDARVD EATQRALHTL TGSARMSGID
SIAVVTKGLE QCIKPLLALD GDLDDGLLTL IRRAVEGIRE RVDELPNLGA GAAALVGLAE
EIAQLAQPVI AGEKIDTPAA SDALPAEIPP EPASEPMSAQ AEAVLGEELE FLLADAEPDA
SAWGWLDEGE GETVEPEASF GETLPEALAD TGDSDQLAGE IVEDAELAAT VVATTQPLSA
VLPGLREDVE TPPPPVIDMT AASWPPSTTL LEAVEPSDAM PAPDPEMAGL FLEDARDLLD
KLDTQFREWQ FAPENIGALD GINRLLHTLK GSARLTGVAA IGDLSHALET RLKALSEEPG
AVNDTTMELA QRAVDTLSAQ IDALEQGAPI PRMSGLIEAL GQAPLEMLDA PVPFPVSPTP
EPFADLANMR EEALQTGAEA PAPSGVEGPV LSGVEGPVPS GVEGPVPSGV EGPVPSGVEG
AVAVPVSPQI RVRSDLLNRL VNHAGEISIY RGRLSQRNGL LGFGLGEFDQ TVARLREQLR
LLEIETQTQI MHRVEREGDV SDYNREFDPL EMDRFSRLQQ LSGSLAETVN DLVSIKDMLG
GYQREFTDLL TQQARLADDL QDGLLRTRLV PFVQVVPRLH RLVRQTADTL GKSARLEVIG
PEVELDRTIL DRLVAPLEHL LRNAVDHGLE DSKTRTANGK PATGKVTLAL RREGNDAVIS
LSDDGKGMDL AAIRQQAIAR GLLAPQTILP DEALLQFILE PGFTTSGKVT QISGRGVGLD
VVASEIKVAN GSIALESVPG QGARFTVRLP LTLAIIEAFL VSAGDNIYAV PHSTVEAAGR
IGRDDLLAIY RGEATEFTSR GHSYKVVYLG GVLDPAQEPD IGERRWLPLL MIRLGEQRVA
LHVDSLLESQ RILVKPLGPQ LAGVRWLSGG TILPDGRVAL ILDALALLRS GAAQLYRPAA
AAVETTKGPL CVMVVDDSLT VRRVTSRLLR RQNMEVLTAK DGVEALTLLD ERMPDLLLLD
IEMPRMDGYE LARHIRRSEG LRDLPIIMIT SRTGAKHREY AMQLGVDRYL GKPYQESELL
NEINSLLAER AG
//
