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Database: UniProt
Entry: A0A0H2M5D4_VARPD
LinkDB: A0A0H2M5D4_VARPD
Original site: A0A0H2M5D4_VARPD 
ID   A0A0H2M5D4_VARPD        Unreviewed;       675 AA.
AC   A0A0H2M5D4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=cheA2 {ECO:0000313|EMBL:KLN52265.1};
GN   ORFNames=VPARA_66410 {ECO:0000313|EMBL:KLN52265.1};
OS   Variovorax paradoxus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN52265.1, ECO:0000313|Proteomes:UP000035170};
RN   [1] {ECO:0000313|EMBL:KLN52265.1, ECO:0000313|Proteomes:UP000035170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBEA6 {ECO:0000313|EMBL:KLN52265.1,
RC   ECO:0000313|Proteomes:UP000035170};
RA   Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA   Daniel R.;
RT   "Genome sequence of Variovorax paradoxus TBEA6.";
RL   Submitted (MAR-2015) 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};
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:KLN52265.1}.
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DR   EMBL; JZWI01000059; KLN52265.1; -; Genomic_DNA.
DR   RefSeq; WP_047787626.1; NZ_JZWI01000059.1.
DR   AlphaFoldDB; A0A0H2M5D4; -.
DR   PATRIC; fig|34073.19.peg.6844; -.
DR   Proteomes; UP000035170; Unassembled WGS sequence.
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; 3.30.70.400; CheY-binding domain of CheA; 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; IPR015162; CheY-binding.
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; PF09078; CheY-binding; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000035170};
KW   Transferase {ECO:0000313|EMBL:KLN52265.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..103
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          286..519
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          521..656
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   MOD_RES         46
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   675 AA;  72025 MW;  FB12C83D3F60C129 CRC64;
     MDLSQFTQAF FVEAVELLAQ MEQLLLELDA EAPDSEQLNA IFRAAHSIKG GAATFGFVAL
     TDTTHLLETL LDRARHGQLK LSRSMIDSFL ETKDALQEQL IAYQAENEPD PERVAHICEV
     LRQLALESDG TQAAPAAAAP VPAAAPVAAA AAVPAQGGAL RIRFSRLSDS ECDLLADELG
     NLGKLLSRTR SGDQLTVVLE TSCAPDDIVA VCCFVIDESQ IDIAAQAAGD AAPAATPVAA
     APSAPAAAAP QPAAAPRATP ASAAAAGAKD SSSIRVDVEK VDQLINLVGE LVITQSMLTQ
     AATMLDPVEC ERFLSGLGHL ERNARDLQES VMSIRMMPMD YVFSRFPRVI RDVSAKLGKE
     VRLDTFGKET ELDKGLIERI IDPLTHLVRN SLDHGIETPS QRIAKGKEAE GQLLLSAQHH
     GGNIVIEVSD DGAGLNRQKI LAKAMQQGLP VTDTMPDDEV WQLIFAPGFS TAEQVTDISG
     RGVGMDVVKR NIQEMGGHVE ISSREGWGTT TRIVLPLTLA ILNGMSVKVG SEAYILPLSY
     VIESLQPRTE HLHSITSDGH VIKVRGEYLP LIELHGVFDV AGAQTDPTQG ILVIVQAGET
     RFALLVDELL GQHQVVVKNL ETNYRKVPGI SAATILGDGS VAFIIDVDAM PRIQRAHAAR
     AAVLAHTART EPVAA
//
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