ID A0A124EB17_9EURY Unreviewed; 781 AA.
AC A0A124EB17;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=APY94_11020 {ECO:0000313|EMBL:KUH32106.1};
OS Thermococcus celericrescens.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=227598 {ECO:0000313|EMBL:KUH32106.1, ECO:0000313|Proteomes:UP000053462};
RN [1] {ECO:0000313|EMBL:KUH32106.1, ECO:0000313|Proteomes:UP000053462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17994 {ECO:0000313|EMBL:KUH32106.1,
RC ECO:0000313|Proteomes:UP000053462};
RA Hong S.-J., Park C.-E., Shin J.-H.;
RT "Draft genome sequence of Thermococcus celericrescens strain DSM 17994.";
RL Submitted (OCT-2015) 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};
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:KUH32106.1}.
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DR EMBL; LLYW01000040; KUH32106.1; -; Genomic_DNA.
DR RefSeq; WP_058939678.1; NZ_LLYW01000040.1.
DR AlphaFoldDB; A0A124EB17; -.
DR STRING; 227598.APY94_11020; -.
DR OrthoDB; 293137at2157; -.
DR Proteomes; UP000053462; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.
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; 2.
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; 2.
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 Kinase {ECO:0000313|EMBL:KUH32106.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:KUH32106.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..111
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 434..645
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 647..779
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 136..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 781 AA; 85770 MW; BB52CFD72EC2F12B CRC64;
MEDLSQYLDE FLADARDRID SLSNAILTLE KIVRDGGSEE EKKAMIDQIF RDAHTLKGTA
ATMSFMKLSE VAHKMENLFD LVRSGKVEPT PELIDVLLEF LDAIEGMVDS IEENGNEGDF
DVEELFAKAE RFFGEGEGAK RESGPAEEAA PPAEPPQVEE SEGGGEAPES EAPEGSIPGR
VYRVRVYFHK DAQLRGIRGF LILSDLEGIG EVLETTPDRS VIEDGKADVD VLEFVIATEE
SPEKIKTIVT RHPEVDDAEV EVQGQAAGEG AKTYTVTVYV QKDAPLKGVR SYLVLQDLQK
IGDVQRTIPD PIAIQNGELI DGRYFRVLLV SNVSQEEISK AVLKHPDVQD VEITEGDVVD
AQRPVQESPS KEKAPRTAET KAPKKKKPPS TPKVKVSKII KVDVGHLDRL MNLVGELVIT
KGRLEQIAER LGDRELLETL STLSRLLTEL QDEIMEMRLT PVAEVFNKFP RMVRELARKM
GKEVEFVIEG ADIEVDRTIL DKLGDVLVHL LRNAIDHGIE APEEREKSGK PRAGRLELIA
RRERSHVEII VKDDGRGIDP EKIKRKALEK GLITPEQAME MSDEEAINLI FLPGFSTKEK
VTDVSGRGVG MDVVKDVVKS LNGSISVQSK VGKGSVFVLK LPVSMAIIQA LLIEVQGEVY
AVPINNILES IEIRRENLKS IGGKEVIVLR GEIIPVVMLH ELFGLPVPEK DEFPAIIIDL
GAQKVAVGVD KLLHKKDIVI KSLGKMLSHI SGFAGATILG DGSVVLIIEI NGLLGGGRGG
L
//
