ID A0A1M6DX02_9RHOB Unreviewed; 628 AA.
AC A0A1M6DX02;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444417_1640 {ECO:0000313|EMBL:SHI77548.1};
OS Wenxinia saemankumensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Wenxinia.
OX NCBI_TaxID=1447782 {ECO:0000313|EMBL:SHI77548.1, ECO:0000313|Proteomes:UP000184292};
RN [1] {ECO:0000313|EMBL:SHI77548.1, ECO:0000313|Proteomes:UP000184292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100565 {ECO:0000313|EMBL:SHI77548.1,
RC ECO:0000313|Proteomes:UP000184292};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQYO01000003; SHI77548.1; -; Genomic_DNA.
DR RefSeq; WP_073328079.1; NZ_FQYO01000003.1.
DR AlphaFoldDB; A0A1M6DX02; -.
DR STRING; 1447782.SAMN05444417_1640; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000184292; 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:SHI77548.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000184292};
KW Transferase {ECO:0000313|EMBL:SHI77548.1}.
FT DOMAIN 1..102
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 283..487
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 489..621
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 215..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 628 AA; 67423 MW; B1AE5A3B547ECD89 CRC64;
MAASADEMFL IEARLLTESL EAGLLDMQER PGDKGLIDSV FRDLHTLKGS GAMFGHAELA
HFLHDFETAF ETVREGKLSV SPPLVKLGLR ACDHAVSLLD GGPPGPGAAL LDELRALVSG
ELPQGAGRPW RLSFRLAPDC LVLGARPQAL LDELRQLGAD EIEPILDDLP ELADLIADRL
YIGWRMTLPP DLTEEAIREV FVFNDEGLAL DLAREGASPD TRPPGEEAGP VAPAGGGARD
RAMMRVPAER LDELMDRVGE LVIAEARLAE LVAADGNPNL VAVSEEIKRL ASGMRETTMS
IRMTPIETIT GRFRRLVHDL NDQLGKTIAL VVEGEETELD KTVIELLADP LLHMIRNSAD
HGLEDAASRL AMGKPATGTI RLSARYSGAE VAITLADDGR GLDLARIRAK AVARGLIPVD
ADLDEAAIRA LILQPGFSTA ESVTELSGRG VGMDVVRRTV DQLRGSVEVD SEPGHGTRIR
MRLPLTLAII DGLLVEIGGE RYSIPLAAVE HIIELPREQA RNSNGMRFLN VRGQLVPFLR
MRDLLASTGD PGPFQKVVVV TAGELRVGLT VDRIIGSSQT VIKQLSPLHS ALKTFSGATV
LGDGSVALIL DVPQLVAFGQ ARDSMEAA
//
