ID A0A1I6QYL9_9RHOB Unreviewed; 703 AA.
AC A0A1I6QYL9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04488040_1082 {ECO:0000313|EMBL:SFS57569.1};
OS Sulfitobacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=394264 {ECO:0000313|EMBL:SFS57569.1, ECO:0000313|Proteomes:UP000199239};
RN [1] {ECO:0000313|Proteomes:UP000199239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23422 {ECO:0000313|Proteomes:UP000199239};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FPAJ01000001; SFS57569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6QYL9; -.
DR STRING; 394264.SAMN04488040_1082; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000199239; Unassembled WGS sequence.
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 Kinase {ECO:0000313|EMBL:SFS57569.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000199239};
KW Transferase {ECO:0000313|EMBL:SFS57569.1}.
FT DOMAIN 1..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 342..552
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 554..690
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 278..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 703 AA; 76242 MW; 72735394BC41DCB7 CRC64;
MSSLTELRAI FFQECEEQLE DLTDGLNAIE AEVEETSPDP DQVNSMFRAV HSIKGGAASF
SLDAIAQFAH AYETILDELR GGQLLTTSDS IPVLYRAADY LADLISLAAA GFEPDPDRLA
LQTSEIMSLS QAEPVAEPEG DFLADFVPLA LDDDGALPVD NGPELPVFNI SFTPTAALYA
NGHEPVQLFR ELETLGRLKV DVELDEQAPW DDPHPAATWR LSLASDRSES DIREIFEFAE
PHAQLQVSLS DGTVDVPQHP MAQTDNAANV QEVEVDDPAG ITEPDTPDSV LPEPTIKPPA
PHKSTVRVDL GQVDELINLV GELVITQSVM TQSLLEHSGP VSRNVMATLD DFKSLTRIIQ
EGIMAIRAQS VKPLFQRMAR IVRETAQMAG KEVRFTSEGE DTEVDRIMIE RLVDPLTHIL
RNAVDHGVEM GPDRLQAGKE EAGCIRLSAA HRSGRVVIEV SDDGAGVKRD KVLASAIAKG
LIQATAQLSE GEIDRLLFMP GFSTADVVTN LSGRGVGMDV VNSEIRRLGG RVSIISSPGE
GTTISISLPL TLAVLDGMIV DVGGETLVVP ISAILETIRP DPSQIHQIGP SSRMVAVRDM
MVPIIELGQV FGYENSSCRR DEHILFIVED ENGTMFALAV DQIRDQRQVV IKSLESNYGH
VPFVAAATIL GDGQIALIVD LDEVTHRISN PPPTSVKHKR AYA
//
