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Database: UniProt
Entry: A9FWB6_SORC5
LinkDB: A9FWB6_SORC5
Original site: A9FWB6_SORC5 
ID   A9FWB6_SORC5            Unreviewed;       572 AA.
AC   A9FWB6;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=cheA4 {ECO:0000313|EMBL:CAN92362.1};
GN   OrderedLocusNames=sce2203 {ECO:0000313|EMBL:CAN92362.1};
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN92362.1, ECO:0000313|Proteomes:UP000002139};
RN   [1] {ECO:0000313|EMBL:CAN92362.1, ECO:0000313|Proteomes:UP000002139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(2007).
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};
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DR   EMBL; AM746676; CAN92362.1; -; Genomic_DNA.
DR   RefSeq; WP_012234837.1; NC_010162.1.
DR   AlphaFoldDB; A9FWB6; -.
DR   STRING; 448385.sce2203; -.
DR   KEGG; scl:sce2203; -.
DR   eggNOG; COG0643; Bacteria.
DR   HOGENOM; CLU_000650_3_7_7; -.
DR   OMA; SEPLMHI; -.
DR   OrthoDB; 9803176at2; -.
DR   BioCyc; SCEL448385:SCE_RS11305-MONOMER; -.
DR   Proteomes; UP000002139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd00088; HPT; 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; 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; 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; 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   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002139}.
FT   DOMAIN          1..105
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          204..406
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          408..539
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          128..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         48
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   572 AA;  60663 MW;  A5B81F7BB4BB3D26 CRC64;
     MDTERAALMQ MFAAETAEHL DELESALLEL ERRPDAGHLL ERIFRVAHTM KGNASSVGAH
     GLSELTHAAE DVIEDLHRGT LPVTGMVVSL LLETVDSARR QLAEMDGGEE PPGSTSLPAS
     VLERLKSARR TEREGTPSTP KGATSSAGDE GDRSPGPKTV RITVEKLDCM VDLIGEVAIT
     RNRIAREVQL AGGAVGAALR DGLEELDRLN TKLEEAIRRA RMVPVGPWFR QYERAVRDLA
     RSHGKLARLV VVAGDVEVDT AVIERLRDAL THLIRNGIDH GLEPPEVRKA CGKDARGTIT
     LRASHEGGGI ALRVSDDGAG MNRAQIAARA SAQGRCPDAD ALSDSELYDL VFEPGFSTAT
     TVSDLSGRGM GMDVVRRRVE SLEGSIGIES AAGVGTTLIL RLPLTLATIE GFSVSAAGER
     YVIPLRAVVA CVGLPRGALA AGPGGVLHVH GRALPCVRLR DLFGLSGPAP ARESVVVVAH
     EGGQAGLVVD SLDGEGRTVI KPLGRLFRRT RGITGSTVLA DGRLALILDV DALMHDLTRG
     RAGGGELALR DRWRAPPSEG RGGAMNPEGR TR
//
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