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Database: UniProt
Entry: A0A160IN11_9BACI
LinkDB: A0A160IN11_9BACI
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ID   A0A160IN11_9BACI        Unreviewed;       669 AA.
AC   A0A160IN11;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ABE65_008735 {ECO:0000313|EMBL:ANC76882.1};
OS   Fictibacillus phosphorivorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1221500 {ECO:0000313|EMBL:ANC76882.1, ECO:0000313|Proteomes:UP000076623};
RN   [1] {ECO:0000313|EMBL:ANC76882.1, ECO:0000313|Proteomes:UP000076623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25-29 {ECO:0000313|EMBL:ANC76882.1,
RC   ECO:0000313|Proteomes:UP000076623};
RA   Zheng Z.;
RT   "Complete genome sequence of Fictibacillus phosphorivorans G25-29, a strain
RT   toxic to nematodes.";
RL   Submitted (APR-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; CP015378; ANC76882.1; -; Genomic_DNA.
DR   RefSeq; WP_066393706.1; NZ_CP015378.1.
DR   AlphaFoldDB; A0A160IN11; -.
DR   STRING; 1221500.ABE65_008735; -.
DR   KEGG; fpn:ABE65_008735; -.
DR   Proteomes; UP000076623; 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   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          263..537
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          539..669
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          256..289
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   669 AA;  73895 MW;  53D90CCC5067C113 CRC64;
     MEMTQYLDIF IEESKEHLQS INQQALLLEK SPGELSIVNE IFRSAHTLKG MSATMGYEDL
     ANLTHCMENV LDAIRNNKLE VSSSVLDVLF ASLDHLEAMV VEISEGGSGK RDVTDTVKEL
     EALEKGEISQ TIQAESKNAA GSLQDYDQYE KQIIIQSKEQ GFHAYELSIS LREDCILKAA
     RVYMVFEVIE QIGEIIKTLP AVDMLETEQF GTHFTLSILT KESAENVKER ILKVSEIDAV
     EVIDIKADQL NISSNSENEE NNKLVHQEVS PQPVKNGEAQ QASNTSSSGK TIRVNIERLD
     QLMNLFEELV IDRGRLEEIS KSLKSLELNE TVERMSRVSG DLQNIILTMR MVPVEQVFNR
     FPRMIRGLAK DLGKKVNLEI VGAETELDRT VIDEIGDPLV HLLRNSIDHG IENPEVRSSK
     GKNETGTIYL RAFHSGNHVF IEIQDDGAGI NKQKVLSKAI ENGILTKEIS ENLTDKQCFE
     LLFASGFSTA DVVSDISGRG VGLDVVKNKI ESLGGSIAVD STEGSGTIFS IQLPLTLSIM
     SVMLVEISRE KYAIPLSSII ETAIIRQEEI LSAHNQKVID FRGKVVPLVN MKDIFEVPGS
     TESNLHVPVV VVRKGDKMAA LVVDSFIGQQ EIVLKSLGQY LTSVFAISGA TILGDGQVAL
     ILDCNALIK
//
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