ID A0A0J1H263_9GAMM Unreviewed; 795 AA.
AC A0A0J1H263;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Phosphorelay protein LuxU {ECO:0000256|ARBA:ARBA00017260};
GN ORFNames=ABT56_09990 {ECO:0000313|EMBL:KLV05856.1};
OS Photobacterium aquae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1195763 {ECO:0000313|EMBL:KLV05856.1, ECO:0000313|Proteomes:UP000036097};
RN [1] {ECO:0000313|EMBL:KLV05856.1, ECO:0000313|Proteomes:UP000036097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12159 {ECO:0000313|EMBL:KLV05856.1,
RC ECO:0000313|Proteomes:UP000036097};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-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};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:KLV05856.1}.
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DR EMBL; LDOT01000012; KLV05856.1; -; Genomic_DNA.
DR RefSeq; WP_047878721.1; NZ_LDOT01000012.1.
DR AlphaFoldDB; A0A0J1H263; -.
DR STRING; 1195763.ABT56_09990; -.
DR PATRIC; fig|1195763.3.peg.2098; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000036097; 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 Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 446..657
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 659..794
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 283..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 795 AA; 84576 MW; 5A56B2B9E99039CC CRC64;
MSFDLDEDIL QDFLIEAGEI LELLSEQLVE LERSPENADL LNAIFRGFHT VKGGAGFLSL
TELVEACHGA ENIFDLLRTG KRSVTPELMD VILEALDTIN VMFGQVQDRE PVEAADPALL
DALHRFSQPP TAEELAQSAP VVEAAAPVVD VPAPVAVEMP PAAPEVVSND APAVMDEQAQ
HAIAGDSVDD ITQDEFERLL DELHGMGKGP SAESDAAIEP ALGAAASVMP SQGSASGDII
SQIQTESGDI TDDEFERLLD ELHGTGKAPG ADDSVIPAAS ATVTDTVKPQ SPVVSNPVSA
AASGDDDLMT DDEFERLLDE LHGAGKGPAA EELEMATMTV AEMIGNDSAD AQLDSLVADL
AAAASQEPAV EPIEIPPSMM AAVAQATAQA APERRAKPAA GKERAKAGDA TVRVDTSTLD
TIMNMVGELV LVRNRLVSLG LNSNDEEMSK AVSNLDVVTA DLQGAVMKTR MQPIKKVFGR
FPRVVRDLAR SLKKDIVLEL RGEETDLDKN LVEALADPLV HLVRNSVDHG IEMPEVREKA
GKPRVGTVLL SASQEGDHIL LTIEDDGGGM DPDKLRSIAV ERGVMDTDAA SRLTDTECYN
LIFAPGFSTK KEISDISGRG VGMDVVKTGI SQLNGSISID SALGKGTRID IKVPLTLAIL
PTLMVGVAKQ PFALPLASVN EIFHLDLRKT NLVDGQLTII VRDKAIPLFY LQDWLCGVGL
PKRERDHGHV VIVQIGHQRI GFVVDTLIGQ EEVVIKPLDE LLQGTPGMAG ATITSDGHIA
LILDVPNLLK HYAGR
//
