ID CHEA_TREPA Reviewed; 812 AA. AC P96123; O83381; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 04-NOV-2026, entry version 154. DE RecName: Full=Chemotaxis protein CheA; DE EC=2.7.13.3; GN Name=cheA; OrderedLocusNames=TP_0363; OS Treponema pallidum (strain DSM 117211 / Nichols). OC Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Treponematales; OC Treponemataceae; Treponema. OX NCBI_TaxID=243276; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSM 117211 / Nichols; RX PubMed=9255518; DOI=10.3109/10425179709034046; RA Greene S.R., Stamm L.V., Hardham J.M., Young N.R., Frye J.G.; RT "Identification, sequences, and expression of Treponema pallidum chemotaxis RT genes."; RL DNA Seq. 7:267-284(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 117211 / Nichols; RX PubMed=9665876; DOI=10.1126/science.281.5375.375; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R., RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A., RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O., RA Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete."; RL Science 281:375-388(1998). 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 (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L- CC histidine.; EC=2.7.13.3; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U61851; AAC45555.1; -; Genomic_DNA. DR EMBL; AE000520; AAC65348.1; -; Genomic_DNA. DR PIR; A71335; A71335. DR AlphaFoldDB; P96123; -. DR SMR; P96123; -. DR STRING; 243276.TP_0363; -. DR EnsemblBacteria; AAC65348; AAC65348; TP_0363. DR KEGG; tpa:TP_0363; -. DR KEGG; tpw:TPANIC_0363; -. DR eggNOG; COG0643; Bacteria. DR eggNOG; COG2198; Bacteria. DR HOGENOM; CLU_000650_3_2_12; -. DR OMA; ACLIMNF; -. DR OrthoDB; 9803176at2; -. DR BRENDA; 2.7.13.3; 6429. DR Proteomes; UP000000811; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:InterPro. DR CDD; cd00731; CheA_reg; 1. DR CDD; cd16916; HATPase_CheA-like; 1. DR CDD; cd00088; HPT; 1. DR FunFam; 2.30.30.40:FF:000048; Chemotaxis protein CheA, putative; 1. DR FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 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; IPR051315; Bact_Chemotaxis_CheA. 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; IPR036890; HATPase_C_sf. DR InterPro; IPR003594; HATPase_dom. 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 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 PROSITE; PS50851; CHEW; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50894; HPT; 1. PE 3: Inferred from homology; KW ATP-binding; Chemotaxis; Cytoplasm; Kinase; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transferase; KW Two-component regulatory system. FT CHAIN 1..812 FT /note="Chemotaxis protein CheA" FT /id="PRO_0000074719" FT DOMAIN 1..111 FT /note="HPt" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110" FT DOMAIN 418..661 FT /note="Histidine kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107" FT DOMAIN 663..798 FT /note="CheW-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052" FT MOD_RES 54 FT /note="Phosphohistidine; by autocatalysis" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107" FT CONFLICT 428 FT /note="G -> E (in Ref. 1; AAC45555)" FT /evidence="ECO:0000305" SQ SEQUENCE 812 AA; 87693 MW; 27EB51B5AD3A557D CRC64; MPMSDYLDAG NEELLKDFFS EAEQQVEQLE SNILVIEQDP TNRDAVDEIF RAAHTLKGGA ATVEMHELSG FTHAVEDLLD GIRSEKVTVD GAVVDLLLTS LDVIKAMLES RAGGGPYAED VSDLVARLRS YLPASGTVPG AARGLSVSSP NAAEAAKGTA VGEDGTEAPQ VGRVPPLSLL SEYDRLELRE IVPPEHSVYA LTVRFDESNL MNTVGGIQVF TALKSCASVL KTVPDFDALY QDMFHEYVVY FVSTVQDSVC VSQVASIPDV TLSVSVAEVA LADLCTPLSE HGELGVCADA GTGGVSEGSG AAVRSGGERV PNSLPKQVAG CAVPSAKDSS KATSSGYGSG SVLRVDAKRI DYLLNLVSET VIIKASLNQS ALEFGEVYTL FQNANGAYKE RLRKFFDRVP AYLEKVKNGQ DADAVRKGMI AEAVGVFDIF SSFENGLKQS VTKFRSSAQN LGRISGELQE GVMKIRMVPI SQIFSRYPRV VRDLSRDLRK EVRLVIEGEE TELDKSVVED LLDPIMHCVR NSLDHGIEAP EVRARSGKPA QGTLLLRASN EGNMIVIEVA DDGRGIDVEA VKTKAVERGV LHPGKNLTEV EAFQLIFAPG FSTSRSVSNV SGRGVGLDVV KTHIERLNGT VSVFSEVQKG TRFVIKLPLT LAIIQGLLIR VGQEVYSIPI ASVIESHRIK SEEINRIDNY EVFNVRNEVI SLLRLDRLFG ISCDDEVTGQ YHYVVIVGAA EKKVGLMVDA LIGEEDVVIK PLRDQFTSSP GIAGASILGD GSVSLIIDVG QLLELGLKRE ILARERREAT VW //