ID A0A0M1P6S4_9BACL Unreviewed; 690 AA.
AC A0A0M1P6S4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AM231_13145 {ECO:0000313|EMBL:KOR89990.1};
OS Paenibacillus solani.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1705565 {ECO:0000313|EMBL:KOR89990.1, ECO:0000313|Proteomes:UP000036932};
RN [1] {ECO:0000313|Proteomes:UP000036932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-22460 {ECO:0000313|Proteomes:UP000036932};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) 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};
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:KOR89990.1}.
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DR EMBL; LIUT01000001; KOR89990.1; -; Genomic_DNA.
DR RefSeq; WP_054402957.1; NZ_LIUT01000001.1.
DR AlphaFoldDB; A0A0M1P6S4; -.
DR PATRIC; fig|1705565.3.peg.4658; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000036932; 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; 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; 3.30.70.1110; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000036932};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 307..557
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 559..690
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 265..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 690 AA; 75637 MW; 269F8A814C40ADB6 CRC64;
MDMNQYLTMF IDESNDHLQS LNENMLQLES NPDDIGIVQI IFRSAHTLKG MAATMGYEDL
ASLTHQMENV LDLVRNEKLK MQDYIFDTLF KSLDALESMV QDITEGGDGK SDVSSIVASL
QSIVRGEGAP SSEGAADGAS PAVSIKGIEL DEFQYSVLDQ SISEGHQVLY IQVTLREDCQ
LKAVRAYMVF EALERSGEIV KTYPDVQEIE QGEFDRVFSL YYITQRETED IDNQIKSISE
IETTSVVALD HESLQQMVQE SAATAEVVKS NDSAATPAPV SPSETTANTN PVKESKASAP
RNTGGGNPSR TIRVDIERLD VLMNLFSELL IDRVRLEQLA SESNNQELTD TVEHMSRVSS
DLQNIVLKLR MVPVDTVFNR FPRMVRDLAK TLDKKIDLII TGAETELDRT VIDEIGDPLV
HLLRNSADHG VEPIADRIAA GKPETGTVHL RAFHSGNNVF IEIEDDGRGI YREKILKNAI
AKGVVTEAEG ASMTDDEVNQ LLFAPGFSTA EKISDVSGRG VGLDVVKSKI VALGGNVTIY
STPGKGTNFS VQLPLTLSII AAMLIQMGSE KYAIPLSSIV ETGIIKRGQI KHVHGSRMVQ
FRESLIPIVS LSRFFDVPDF DEEAEEETEI VVIRKGDRLA ALTIDDFIGQ SEIVIKNLGK
YLPAIQGISG ATILGDGQVA LIIDANAFIK
//
