CHEA_TREPA
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 25-MAY-2022, entry version 140.
DE RecName: Full=Chemotaxis protein CheA;
DE EC=2.7.13.3;
GN Name=cheA; OrderedLocusNames=TP_0363;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=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=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}.
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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.TPANIC_0363; -.
DR EnsemblBacteria; AAC65348; AAC65348; TP_0363.
DR KEGG; tpa:TP_0363; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_2_12; -.
DR OMA; MMDMAKS; -.
DR BRENDA; 2.7.13.3; 6429.
DR Proteomes; UP000000811; Chromosome.
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; cd00088; HPT; 1.
DR Gene3D; 1.10.287.560; -; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.30.70.1110; -; 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; SSF47226; SSF47226; 1.
DR SUPFAM; SSF50341; SSF50341; 1.
DR SUPFAM; SSF55052; SSF55052; 1.
DR SUPFAM; SSF55874; SSF55874; 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
