ID A0A148KNY3_9ALTE Unreviewed; 724 AA.
AC A0A148KNY3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AX660_20805 {ECO:0000313|EMBL:KXI27948.1};
OS Paraglaciecola hydrolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI27948.1, ECO:0000313|Proteomes:UP000070299};
RN [1] {ECO:0000313|EMBL:KXI27948.1, ECO:0000313|Proteomes:UP000070299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S66 {ECO:0000313|EMBL:KXI27948.1,
RC ECO:0000313|Proteomes:UP000070299};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXI27948.1}.
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DR EMBL; LSNE01000009; KXI27948.1; -; Genomic_DNA.
DR RefSeq; WP_068379794.1; NZ_LSNE01000009.1.
DR AlphaFoldDB; A0A148KNY3; -.
DR STRING; 1799789.AX660_20805; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000070299; 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:SF1; 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:UP000070299};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 371..582
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 584..721
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 126..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 724 AA; 77796 MW; AB59F909958A62F8 CRC64;
MAFDVDEDIL QDFLVEAGEI LELLQEQLVD LENNPEDGGL LNAIFRGYHT VKGGAGFLSL
TELVDICHGA ENVFDVMRTG QRTLTPELMD VILQATDEVV KMFSSVKAGK PLVAAEQDLL
DTLHRLSRPE SEDEVVDDEE SVAPSTDEDH EPVAVVAEKE SGDFSEDEFE ALLDELHGKA
APGAKDAVVE KKSPAKSGAD EDISDDEFEA LLDQLHGKGQ FKAENEVPLP AKPVEAAKSN
KAKSGDDEIT DEEFEALLDQ LHGKGQAPDT VEAEKPAAPK PTENKPAASA AKPVAPVAKK
APAPVVKKAP ESAPASGDSD SKEDKKSGGA PQAETTVRVD TKRLDQIMNM VGELVLVRNR
LISLGININD ESMSKAIANL DVVTGDLQGA VMKTRMQPIK KVFGRFPRVV RDLARTLKKE
ITLELEGEET DLDKNLVEAL ADPLVHLVRN SVDHGIEMPE DRKAAGKPTM GTVKLAASQE
GDHILLTITD DGKGMDPEKL KEIAIKRGVM DADTAARMTD VEAFNLIFAP GFSTKTEISE
VSGRGVGMDV VKTKINQLNG TVKIDSKMGV GTILEIKVPL TLAILPTLMI VVGEQTFALP
LGSVNEIINV DPTKTNTVDG QLTMIVRSKA IPLFYLREWL TRTPGKHGII DKTKGHVVVV
QIGTKQLGFV VDALIGQEEV VIKPLDELLQ GTPGMAGATI TSDGGIALIL DVPGLLKRYA
AKRG
//
