ID A0A1I5UM19_9LACT Unreviewed; 678 AA.
AC A0A1I5UM19;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04488506_0066 {ECO:0000313|EMBL:SFP96219.1};
OS Desemzia incerta.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae; Desemzia.
OX NCBI_TaxID=82801 {ECO:0000313|EMBL:SFP96219.1, ECO:0000313|Proteomes:UP000199136};
RN [1] {ECO:0000313|EMBL:SFP96219.1, ECO:0000313|Proteomes:UP000199136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20581 {ECO:0000313|EMBL:SFP96219.1,
RC ECO:0000313|Proteomes:UP000199136};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOXW01000001; SFP96219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5UM19; -.
DR STRING; 82801.SAMN04488506_0066; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000199136; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding 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; IPR037052; CheA-like_P2_sf.
DR InterPro; IPR010808; CheA_P2-bd.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR035891; CheY-binding_CheA.
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 Pfam; PF07194; P2; 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; SSF55052; CheY-binding domain of CheA; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Kinase {ECO:0000313|EMBL:SFP96219.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000199136};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 292..538
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 540..671
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 678 AA; 74766 MW; D57178B94C6519E8 CRC64;
MDDNSKYLEL FFEESDEHIQ SLNDCVLDLE SDPENQEIID DMFRSAHTLK GMAGTMGYDS
LAQLTHKMEN VFDLLKKKII KADSRSIELI FSCLDSISAI VEDLRQGGEG VLDVADLVVR
LNAISEGEQD VSVEEKTVAE SDDNFNSQLH FIDESDVAVI ESAAADGYQA YTVTIKIEET
SGMKNARVFL VMSKLDQQGE VLHSEPNAEV LENEDFGSIF KVVLLTQADE ETLKEAALNN
SEIEDVLVKE FDSNDVVSEK EIEEKVVLEA KAVPVEEAKK ETVKKTASKS TQSNQTVRVD
ITKLDDFLNA VSELLIYRTR LESISQDNEI KEMNEPLEQF ARITTELQDL VLKIRLQPVS
TVMTNFPRMI RDLGNDLGKK YNLVIEGGET ELDRTVVSEL GEPLIHLIRN AADHGIEMPE
DRQKIGKDPA GLIHISAYQE GNRVVLTVRD DGKGLNPQAI KESAERKGIV TTGLSDLELQ
HLIFHPGFST AKEVTGISGR GVGMDAVQQK IHSLGGTVEI ISAINQGTTF KINLPLTLSI
IDSLLIKVGD STFAIPRGII EKVVSPGPGE IIQTYENEIY TTGGATPVIR LTEVLGMEET
NNPEPYLIIV KLGENRFALK IDDIIKQQEI VIKDLGKELS QVNCYSGATI LGNGEIVLIL
DVTAIANESQ GVQNAIRV
//
