ID F5Z5C8_ALTNA Unreviewed; 702 AA.
AC F5Z5C8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=ambt_16745 {ECO:0000313|EMBL:AEF04854.1};
OS Alteromonas naphthalenivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF04854.1, ECO:0000313|Proteomes:UP000000683};
RN [1] {ECO:0000313|EMBL:AEF04854.1, ECO:0000313|Proteomes:UP000000683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC {ECO:0000313|Proteomes:UP000000683};
RX PubMed=21705606; DOI=10.1128/JB.05252-11;
RA Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA Oh T.K., Kim J.F.;
RT "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT bacterium Alteromonas sp. strain SN2.";
RL J. Bacteriol. 193:4292-4293(2011).
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; CP002339; AEF04854.1; -; Genomic_DNA.
DR RefSeq; WP_013785775.1; NC_015554.1.
DR AlphaFoldDB; F5Z5C8; -.
DR KEGG; alt:ambt_16745; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_6; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000000683; 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
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..558
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 560..694
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 131..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..169
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 702 AA; 75973 MW; DEF1F9DED28BAAAD CRC64;
MSIDIEQFHG VFFDESDEHL DDMEQLLISL DVDSPDPEEL NSIFRAAHSI KGGSGIFGFN
ALMNLTHVME NLLDKARNQE ISVTTNIVNL LLETLDVLKA TLSAYRDQVD VPEQAIAVSI
TKLERALSET QGAAAADTSN DVDNANGFDN SNGSSDADSS DSSNDNSDAF GFFDDEPDLT
TNISQQTEIN DVELSTQSDD GFGFFDDTPS EAVASAEDDG FGFFDEPEMQ VSTPVASDNS
YGFFDTTELP ENKATPDNSE AVISPKLFVL DPIAAKGTGE TSALKKKSPP KASDSAPPIK
TNKKSVGRDS ASIRVDTKKI DSMVNLVGEL VITQSMLSMI GQEVDGQVGE RLQVAIDELQ
RNTREIQESV MSVRMLPLTA TFNRFPRLVR DLAGKLDKKV DLVLQGAHTE IDKSLIEKLV
DPLTHLVRNS IDHGIELPEK RRAAGKPEMG TVILGAEQKG GSIIIKIIDD GGGLNRARIL
EKARSNGLTV DDDMPDSEVW QLIFQAGFST AEAVTDVSGR GVGMDVVRRN IEAIGGRIEI
ESSLGEGSGF FIHLPLTLAI VDGMCASVGN QIFVIPLLNI VESFQPTASQ LKTLGNDTVL
YVRDQYWPLV PLHDYMDVEN ANRKPTEAIV VLLESSKKRF GVLVDALVGQ QQVVIKSLEA
HYRKVAGLAG ATIMGDGKVA LIIDADSIAT TYTSSQLEDM LA
//
