ID H9UAS3_FERPD Unreviewed; 681 AA.
AC H9UAS3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Ferpe_0477 {ECO:0000313|EMBL:AFG34616.1};
OS Fervidobacterium pennivorans (strain DSM 9078 / Ven5).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=771875 {ECO:0000313|EMBL:AFG34616.1, ECO:0000313|Proteomes:UP000007384};
RN [1] {ECO:0000313|Proteomes:UP000007384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9078 / Ven5 {ECO:0000313|Proteomes:UP000007384};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Noll K.M., Woyke T.;
RT "Complete sequence of Fervidobacterium pennivorans DSM 9078.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003260; AFG34616.1; -; Genomic_DNA.
DR RefSeq; WP_014451082.1; NC_017095.1.
DR AlphaFoldDB; H9UAS3; -.
DR STRING; 771875.Ferpe_0477; -.
DR KEGG; fpe:Ferpe_0477; -.
DR PATRIC; fig|771875.3.peg.486; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_0; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000007384; Chromosome.
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: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 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFG34616.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:AFG34616.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 298..548
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 550..681
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 275..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..42
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 681 AA; 76437 MW; D2E626459A5443A9 CRC64;
MGEYNEYLSV FIDESKEYIQ LLNEALLELE KNTSDVEQIN RAFRALHTLK GMAGTMGFER
LAKLCHRMEN YLDAVRSGKV EITSDELDYL FAGLDMIEKM LKAIVEHGSD ELDESSEGLV
EVFERIAKGE KVEKSGRKID KSEFGEVKET KEKTSAETST KVFTESFTQE VLRDVLEEAE
KKGVPAYHIV VNLQEGTQLK SARMYMVFHA LEEIGVEIVH SIPPVEDIEN EKFDLTVELI
GIGNVPQEKI YEKIMGVSEI KSVIVKPLKI EEKKKETAVG SETKEPEEQS VKEQKRTKIT
QTVRVDTEKL DTLMNLMGEL VIARSRIADI LKKYNIKEVD ESLAQLSRIT LDLQNIVMKV
RMVPIEFVFN RFPRVVRDLA RNLGKEINFI MEGEETELDR TFVEVIGDPL VHLIRNAIDH
GIETKEERIA LGKPPIGTVK LSARHEGNNV VIEVEDDGRG LNREKILRKA IERGLITEEK
AATLPDEKVF DFIFLPGFST KDQVSELSGR GVGMDVVKNT IESLNGSVSI ESKPGKGTKV
TIRLPLTLAI IQALLVKVNN YVYAIPISII DSTLIISPEE IKVVQNEEVI VIRGEVIPLI
KLWHVFNFPH EETPSEMKVV VVKHGNRKYG LTVDTLIGQE DIVIKSLGKI FSDVKIFSGG
ATLGDGSIAL ILDVANIVEM A
//
