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Database: UniProt
Entry: A0A2S0U944_9BACL
LinkDB: A0A2S0U944_9BACL
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ID   A0A2S0U944_9BACL        Unreviewed;       691 AA.
AC   A0A2S0U944;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DCC85_08835 {ECO:0000313|EMBL:AWB44315.1};
OS   Paenibacillus sp. CAA11.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1532905 {ECO:0000313|EMBL:AWB44315.1, ECO:0000313|Proteomes:UP000244407};
RN   [1] {ECO:0000313|EMBL:AWB44315.1, ECO:0000313|Proteomes:UP000244407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAA11 {ECO:0000313|EMBL:AWB44315.1,
RC   ECO:0000313|Proteomes:UP000244407};
RA   Um Y., Kim S., Gong G.;
RT   "Complete genome of CAA11.";
RL   Submitted (APR-2018) 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; CP028922; AWB44315.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0U944; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000244407; Chromosome.
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:UP000244407};
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          308..558
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          560..691
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          266..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   691 AA;  75583 MW;  27BFCCB78D7FAD51 CRC64;
     MDMNQYLSMF IDESNDHLQA LNDNMMQLED NPEDISIVQV IFRSAHTLKG MAATMGFEDL
     ASLTHQMENV LDLVRNDKLK MQDFIFDTLF KSLDALQSMV QDITEGGEGK ADVTSIVDSL
     QAIVRGEVPG EAKASAPAKA PAASANSSIV LDEFQYSVLE QSIAEGHKVL YVDVVIRDDC
     QLKAVRAYQV FDLMERNGEV VKSFPSAQDI EQDKFDRSFS LYYITQKEAE ELKNLILNIS
     EISEAKVVQL DAETLQQMAL PQAEAAAAVE APPAAPQPEK AEKSSAPAPA KSKGAEAAPK
     RAGGGTPAPS RTIRVDIERL DVLMNLFSEL LIDRVRLEQL AGEIKRSELT ETVEHMTRVS
     GDLQNIVLKL RMVPVDTVFN RFPRMVRDLA KSLDKKIDLI ITGAETELDR TVIDEIGDPL
     VHLLRNAVDH GVETTAERIE AGKPETGTVQ LRAFHSGNHV FIEIEDDGKG IDREKVAAKA
     IKNGVITEEQ AQAMTDDEVA LLLFAPGFST AEKISDISGR GVGLDVVKSK IESLSGTVQV
     TSKLGSGSKF SVQLPLTLSI ISAMLIKTGE EKYAIPLSSI VETGMIKRAQ IREIHGYKMI
     PYRDTNIPLL SLAEIFDVPG YDESQEVETE IVVIRKGDRL AALTVEEFVG QNEVVIKNLG
     KYLPSIQGVA GATILGDGQV ALIIDPNAFI K
//
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