ID A0A1G6JNB8_9PROT Unreviewed; 857 AA.
AC A0A1G6JNB8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04487779_1001228 {ECO:0000313|EMBL:SDC20187.1};
OS Belnapia rosea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Belnapia.
OX NCBI_TaxID=938405 {ECO:0000313|EMBL:SDC20187.1, ECO:0000313|Proteomes:UP000198925};
RN [1] {ECO:0000313|EMBL:SDC20187.1, ECO:0000313|Proteomes:UP000198925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 100156 {ECO:0000313|EMBL:SDC20187.1,
RC ECO:0000313|Proteomes:UP000198925};
RA de Groot N.N.;
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; FMZX01000001; SDC20187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6JNB8; -.
DR STRING; 938405.SAMN02927895_00413; -.
DR Proteomes; UP000198925; 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; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.40.50.180; CheA-289, Domain 4; 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; IPR011006; CheY-like_superfamily.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 2.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 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 SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 2.
DR SUPFAM; SSF52172; CheY-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; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SDC20187.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000198925};
KW Transferase {ECO:0000313|EMBL:SDC20187.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 177..428
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 430..566
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 591..720
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 735..852
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 147..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 785
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 857 AA; 90716 MW; 91D8345857020E07 CRC64;
MDDLLTDFLT ETQEGLGALD AALVRLERAP EDMATLSEVF RIVHTIKGTC GFLGLTRMEG
VAHAAENVLG RYRDGTLRAT QAGISVILGA IDCIRGIVAA LEGTGTEPEG DDASLIAALD
AVAGGDAIAP PPVVAPIAVT APAAEAEPPP ARAPAAMVPA APQAAPPATE PESAGANAPP
QTIRVTVEVL EGLMMLVSEL VLTRNQLLQL SRNGADNAFA VPLQRLSHIT SDLQEGVMKT
RMQPIGNAWA KLPRLVRDLG VELGKKIELE MRGAETELDR QVLELIKDPL THMVRNSADH
GLETPEQRVA AGKPEAGRIM LNASHEGGHI IIEIADDGRG LNAERIRQKV LAQGLATEAE
LAAMPEREIQ RFIFRAGFST AAAVTAVSGR GVGMDVVKTN MERIGGTIEV RSKEGRGTAF
IVKIPLTLAI VSALIVEAGG ERFAIPQIGV VELVRVGGEG APQLERIKDS AVLRLRDRLL
PLVNLAGLLQ LESSATEESA FVIVTQVGAH VFGIIVDRVF DTEEIVVKPV APILRHVTMF
SGNTILGDGS VIMILDPNGI ARATGVGAES GEGEAERDGK RQVIAHRSDQ RTALLLFRAG
DATPKAVPLG LVARLEDVER ARIENAGGRP LVQYRGKLMP LVPMSGHWDQ AMAPERQPVL
VFSDGDRTMG LMVDEILDVV EEVMTIDGAG ERPGFLGTTV IGGKVTEMLD TAWWLRQAGE
DWFGGAEPAA GAGRRILLVE DSAFFRNLVV PAIGAAGYAV TAVPDAEEAL RLREAGASFD
AVISDIAMPG MDGFALAHAL RESGPWRSLP LIALTGCSDP ADIERGRAAG FTDYVAKFDR
AALLDSLRQC LSAPVAG
//
