ID A0A0H3J1Q1_CLOPA Unreviewed; 687 AA.
AC A0A0H3J1Q1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:AJA51819.1};
GN ORFNames=CLPA_c17610 {ECO:0000313|EMBL:AJA51819.1}, CP6013_01420
GN {ECO:0000313|EMBL:KRU12173.1};
OS Clostridium pasteurianum DSM 525 = ATCC 6013.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA51819.1, ECO:0000313|Proteomes:UP000030905};
RN [1] {ECO:0000313|EMBL:AJA51819.1, ECO:0000313|Proteomes:UP000030905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 525 {ECO:0000313|EMBL:AJA51819.1}, and DSM 525 / ATCC 6013
RC {ECO:0000313|Proteomes:UP000030905};
RX PubMed=25700415;
RA Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.;
RT "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing
RT Clostridium pasteurianum DSM 525.";
RL Genome Announc. 3:e01591-e01514(2015).
RN [2] {ECO:0000313|EMBL:KRU12173.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU12173.1};
RA Pyne M.E., Utturkar S.M., Brown S.D., Moo-Young M., Chung D.A., Chou P.C.;
RT "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT 6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KRU12173.1, ECO:0000313|Proteomes:UP000028042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU12173.1,
RC ECO:0000313|Proteomes:UP000028042};
RX PubMed=25103768;
RA Pyne M.E., Utturkar S., Brown S.D., Moo-Young M., Chung D.A., Chou C.P.;
RT "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT 6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL Genome Announc. 2:0-0(0).
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; CP009268; AJA51819.1; -; Genomic_DNA.
DR EMBL; JPGY02000001; KRU12173.1; -; Genomic_DNA.
DR RefSeq; WP_003443829.1; NZ_JPGY02000001.1.
DR AlphaFoldDB; A0A0H3J1Q1; -.
DR GeneID; 76626177; -.
DR KEGG; cpae:CPAST_c17610; -.
DR KEGG; cpat:CLPA_c17610; -.
DR PATRIC; fig|1262449.3.peg.1597; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR Proteomes; UP000028042; Unassembled WGS sequence.
DR Proteomes; UP000030905; 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 Kinase {ECO:0000313|EMBL:KRU12173.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000030905};
KW Transferase {ECO:0000313|EMBL:AJA51819.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 312..558
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 560..687
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 130..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 687 AA; 77110 MW; 31A2A5BC12566AD0 CRC64;
MDTSQYLSMF LEESMDNLQT LNESLLELEQ EPEDIDKLNE IFRVAHTIKG MAATMGFNRM
AELTHKMEDV LSEFRNGELK VTQEVVTVLF KCLDTLEQMV DNISNGEEEE MPVEDIIDKL
EHISNNVKNS SEEIAAKEPQ QEETVKSEKS PKEDPKASKI DLNEYDINII KQAVERGYNA
LEITIVLSET TLLKSARAFL IIKALEENGE IIKSIPSTED LENENFDFEI QLIYLTEKSE
EDTKKVLESI SEIDKIVVVP VKQDAVKASN ASVKEETVKK EEPKPVKSEA KVSASNVPKK
PAENHKKENH KKVHQSVRVE LDRLDKFLNM VSELVINRTR LEQISSNYKL VELNETIEQV
ARTTNDLQDL VMKIRMLPLD TVFNRFPRMV RDLSVELNKE IELIIEGQDT ELDRTVIDEI
GEPLIHLIRN SADHGIETKE ERLSRGKDEV GTIKLIAYQE GTKAVIKVQD DGAGIDVEKV
QEKAEKVGIN TDGMNENDIR NLIFAQGFST NEVVTDISGR GVGMDVVKTK ISALGGTVDL
TSEEGKGTTF TIKLPLTLQI ITALLVKVGE ENLAISLNYI DSVIDYKEED IKRTNNKEVI
IYRDKVLPII RVNEKLGIPK TDKDRVYIVI VNVGEKSAGL LVDSLEGQQD IVIKPLGKTL
KGLKEYIGAT ILGDGLVTLI LDVGAFV
//
