ID A0A251X2R4_9RHOB Unreviewed; 736 AA.
AC A0A251X2R4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BVC71_03740 {ECO:0000313|EMBL:OUD10614.1};
OS Marivivens niveibacter.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Marivivens group; Marivivens.
OX NCBI_TaxID=1930667 {ECO:0000313|EMBL:OUD10614.1, ECO:0000313|Proteomes:UP000194664};
RN [1] {ECO:0000313|EMBL:OUD10614.1, ECO:0000313|Proteomes:UP000194664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A06712 {ECO:0000313|EMBL:OUD10614.1};
RA Hu D., Wang L., Shao Z.;
RT "The draft genome sequence of HSLHS2.";
RL Submitted (DEC-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:OUD10614.1}.
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DR EMBL; MSPP01000001; OUD10614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251X2R4; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000194664; 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000194664}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 356..601
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 603..736
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 310..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 736 AA; 79787 MW; 80DF97211F26CBF1 CRC64;
MNSLLDQFVS ECRDLIETSS RALLALETDT ENPAQINELF RAIHTIKGAS GLFDFKPLTS
CVHAGEDLLD AVRAGDVAFN SGIADLLLEM LDRLVEWLDS IEDSETLPSD AQEISAALST
RLRDYISDGA GVNDADDTSQ QTEVAAPWPD DIPVLEGAET GLSLITYTPG ETTFFAGGDP
LRTVLAAPGL LWMQVVQPDD WPDVDQLDPF MLKIGFRLVS SATVPDLEKH FSYDIDDVSI
ERIAATDGPS AIEQLADDIL QSQAALLATP QTGVAAENIQ KSAADVVARV GRNLNVSDDA
VGDLDATIAD VRGEPAGNDP APVDKPQVAE PEKQPAAAPA KQRSSGYLRV DSDRIDALMN
LAGELIVAKN AMPFLARKAE NIEDGRELVR EIKMQHNTIN RIAEELQAAI MQIRMVPVGS
VLSRFNRLVR DMSRKLGKDI RYVVDGEDTE ADKAIVDELS DPIVHLIRNS IDHGIEDPTE
RAEADKPKQG TIRVSAFNKD DSVVIEITDD GKGIAVDKVV KKALERGLID AERVNAMSAN
EKLQLIFLPG LSTKEEVSDL SGRGVGMDVV ASMVRRLGGQ ISIDSEPGLG ARVTLSLPLS
MAVQQLMMVE VGDGLYGVPV DSVVESQKIS PVSIRRHRDA EMVLLRDRLI PLVRMRDLFQ
CDAQDDPETL SVMVVDVNGH ESGLVVDRFH PGVDAIVKPM SGVLANYDCY SGTALLGDGS
ILLALNLREI VECQYH
//
