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Database: UniProt
Entry: K2CNX0_9BACT
LinkDB: K2CNX0_9BACT
Original site: K2CNX0_9BACT 
ID   K2CNX0_9BACT            Unreviewed;       764 AA.
AC   K2CNX0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ACD_35C00294G0003 {ECO:0000313|EMBL:EKD87672.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD87672.1};
RN   [1] {ECO:0000313|EMBL:EKD87672.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EKD87672.1}.
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DR   EMBL; AMFJ01013302; EKD87672.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2CNX0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding 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; IPR037052; CheA-like_P2_sf.
DR   InterPro; IPR010808; CheA_P2-bd.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR035891; CheY-binding_CheA.
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:SF10; 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   Pfam; PF07194; P2; 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; SSF55052; CheY-binding domain of CheA; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          2..106
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          369..627
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          629..763
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   764 AA;  84166 MW;  256F4EDB6819AC05 CRC64;
     MAFDISEDEL PIFQAETEDH LTTLEDGLVR LEQDDRDPEL LQALFRAAHT IKGTAGMIGH
     KRLVEITHVL ENAFDAVRKS QLPISTNLID LCLETVDILR SLRDEVITNE SCVCDVPQMI
     ETFKTFLDSA MNSSRDNKET DVVKVKSNTS VVKPERKPAD LAQSKNRKID AEMSEIGENE
     ESVKELHIEV DISSTSVASA ARAFQILMIL QNAGEIVDLI PTQESIESAA PVGHLSARII
     PGKSEEEIKK EILNIPEIDR LVFKNEVISL VDVSVMNETL TNVEQPEIEV SRLGEHLLSK
     NLISAADLKT VLEKQRSYPP DSAPLLGQLL VSMGFLSQSV VDQAIEETMN QKRSAILSGG
     DAAKAGEHLV DRTVRTSVER LDALMNLVGE LITDRNRLIK IHSAFERDFR GNENTNTLSE
     AVVHIGRITD QLQEEVMHIR MLPVANVFKK FPRMVRDMAQ KVGKEIDLVI RGQETELDRS
     VIEEINDPLI HLIRNSVDHG VETPEKRLEV GKDKRGTIIL SARHDQGRIV ITVEDDGGGI
     NVSKIKAASV RKGVITQAEA DGMSDEKAID LIFESGLSTA EKVTDISGRG VGMDIVRSNI
     ERLNGSILVD SVPGKGSQFQ IILPLTLAIV PTLLVKVHES IFAIPLVTVV ETQKLVDQKF
     QTVNGKSVVV LREKIIPLIK LADVFDLVEE KHITNYSYVV VVRTSKQEVG IVVEHLVGEE
     EVVVKSFGHV IGDIQGVSSA AILGDGQIAL IVDVQGLIKL SSNH
//
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