ID H9ULL3_SPIAZ Unreviewed; 699 AA.
AC H9ULL3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Spiaf_2374 {ECO:0000313|EMBL:AFG38406.1};
OS Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG38406.1, ECO:0000313|Proteomes:UP000007383};
RN [1] {ECO:0000313|Proteomes:UP000007383}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC {ECO:0000313|Proteomes:UP000007383};
RX PubMed=23991249; DOI=10.4056/sigs.3607108;
RA Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT Rift.";
RL Stand. Genomic Sci. 8:165-176(2013).
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; CP003282; AFG38406.1; -; Genomic_DNA.
DR RefSeq; WP_014456388.1; NC_017098.1.
DR AlphaFoldDB; H9ULL3; -.
DR STRING; 889378.Spiaf_2374; -.
DR KEGG; sfc:Spiaf_2374; -.
DR PATRIC; fig|889378.3.peg.2349; -.
DR eggNOG; COG0643; Bacteria.
DR HOGENOM; CLU_000650_3_7_12; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000007383; 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; 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 InterPro; IPR037257; T2SS_E_N_sf.
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; SSF160246; EspE N-terminal domain-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 Kinase {ECO:0000313|EMBL:AFG38406.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000007383};
KW Transferase {ECO:0000313|EMBL:AFG38406.1}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 369..572
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 574..699
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 132..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 699 AA; 76367 MW; 0721CD6985AA2F93 CRC64;
MKTETDPLEI FREEAAEILS EFEQTLINLE EAPANLELVD AAFRHLHTLK GAASMFGFNG
LVEVTHLLEA LFEQIRNTGA AVSSEAVSTA LRSRDEITRL VQAALDGAGD DTANQSIIAD
ITRLMASGAD AAGSTAGSGG SGQAPAGVLS DDAPGEQRST RTFRIEYTPH PDVLKNGGNP
LSLLQELGEL GTTLVIGFCS RVPELAELDP EQCYIGWEIL ITTDRSEDEL RDVFLFAQDS
RKLEFVLIDA EELGDSNLSY KRLGELLVER GDIQPDQLAS VMQDRDFLGQ LLVEKGYVTG
ERLQSALEEQ QYVRKLRETR QKVELSSTIK VRTDKLSALV NLVGELGTLH ARMGLLAHRR
QDEDMFTVSE QLESMLRQLR ELAMEMHMVP VGLLFNGFRR LVRDLAADLG KEVRLVQEGT
EAELDKNVLD KLKDPLLHII RNSIDHGIES PARRRELGKP EEGTLTLRAQ YSGASVLIEV
QDDGAGLNSE KIRAKAVERG LIDAGQELSQ EEIYDLIFEP GFSTADVATN VSGRGVGMDV
VRSNLESISG SVSIRSEPGQ GSTLSLRIPL TLAILEGLLA PVAGQRYLVN LANVVECVDL
AEYDHDEDAG LVTYRGSKLP LLNIARMFGF SGQAESVYML VVTNGQRKLG LAIDAVPSSY
QGVVKPLGRM FSRHEGFSGA VMLGDGTPAL VLDVERLFR
//
