ID A0A127FAK5_STEDE Unreviewed; 732 AA.
AC A0A127FAK5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ACG33_05840 {ECO:0000313|EMBL:AMN46625.1};
OS Steroidobacter denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Steroidobacterales;
OC Steroidobacteraceae; Steroidobacter.
OX NCBI_TaxID=465721 {ECO:0000313|EMBL:AMN46625.1, ECO:0000313|Proteomes:UP000070250};
RN [1] {ECO:0000313|EMBL:AMN46625.1, ECO:0000313|Proteomes:UP000070250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18526 {ECO:0000313|EMBL:AMN46625.1,
RC ECO:0000313|Proteomes:UP000070250};
RA Yang F.-C., Chen Y.-L., Yu C.-P., Tang S.-L., Wang P.-H., Ismail W.,
RA Wang C.-H., Yang C.-Y., Chiang Y.-R.;
RT "A Comprehensive Approach to Explore the Metabolic and Phylogenetic
RT Diversity of Bacterial Steroid Degradation in the Environment: Testosterone
RT as an Example.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011971; AMN46625.1; -; Genomic_DNA.
DR RefSeq; WP_066919505.1; NZ_CP011971.1.
DR AlphaFoldDB; A0A127FAK5; -.
DR STRING; 465721.ACG33_05840; -.
DR KEGG; sdf:ACG33_05840; -.
DR PATRIC; fig|465721.4.peg.1245; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000070250; 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; 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; 3.30.565.10; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AMN46625.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000070250};
KW Transferase {ECO:0000313|EMBL:AMN46625.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 350..591
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 593..728
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 132..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 381..408
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 285..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 732 AA; 78444 MW; 5C772274E5CD6675 CRC64;
MAIDLAQFHD AFFDESFEAL DQMESALLKL NPGAPDPELI NTIFRVAHSI KGGSATFGFS
EVASFTHTCE TLLDELRGNR MQVTRPITDL LLKSVDVMRE MLRAVQHKEP IDAQRVADLQ
FDLELTIAQK DNAPAASPTP TPTPAAAASQ PESLSAPVAQ ALPESLMARR WRIQFKPYPQ
LFAHGNDPLR MLRELAEIGD LTVTARSEDL PPLTELEPES CYLSWDLTLD TEVTREVIAQ
VFDWAEGDCE LHIEQDSASS DGLSAGDSGI DAVRPLASPA ASAEPTSAPA GNSPSAGAPT
GAAASGNVVS LVGEARPAVE PARGTSTPAE GTEGAKSGLG DASSIRVSTD KIDELMNIVG
ELVITQSMLT QLGATIPGHV AEQLRSGLAQ LERNVRELQE SVMRVRMLPI SFVFSRFPRM
VRDVSQRLGK QVALKMTGDQ TELDKTILEK IGDPLVHLVR NSVDHGIEQP EVRLAAGKPA
HGTVYLEAYH KGGNITVEVS DDGGGLDKEK ILAKARARGI VGANEVLSDE AIHDLIFGAG
FSTAEQTTDI SGRGVGMDVV RRNIKELGGT IEVRSTPGAG SRFIITLPLT LAIVDGQSVA
VGTETYIVPL ITIIESLQLK PGMVNRVAGQ GEVFWFRDAY VPVMRLHEVF GVQPRTTQLH
EGLIMVVEGE GRKVGLFVDD LLGQQQVVIK SLESNFRRVD GVSGATILGD GAVALILDVS
GLVRVAMQRV AA
//
