ID A0A017RXU9_9CLOT Unreviewed; 656 AA.
AC A0A017RXU9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Q428_05825 {ECO:0000313|EMBL:EYE88770.1};
OS Fervidicella metallireducens AeB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Fervidicella.
OX NCBI_TaxID=1403537 {ECO:0000313|EMBL:EYE88770.1, ECO:0000313|Proteomes:UP000019681};
RN [1] {ECO:0000313|EMBL:EYE88770.1, ECO:0000313|Proteomes:UP000019681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AeB {ECO:0000313|EMBL:EYE88770.1,
RC ECO:0000313|Proteomes:UP000019681};
RX PubMed=24786951;
RA Patel B.K.;
RT "Draft Genome Sequence of Fervidicella metallireducens Strain AeBT, an
RT Iron-Reducing Thermoanaerobe from the Great Artesian Basin.";
RL Genome Announc. 2:e00345-14(2014).
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:EYE88770.1}.
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DR EMBL; AZQP01000013; EYE88770.1; -; Genomic_DNA.
DR RefSeq; WP_035379002.1; NZ_AZQP01000013.1.
DR AlphaFoldDB; A0A017RXU9; -.
DR STRING; 1403537.Q428_05825; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000019681; 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:UP000019681};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 281..527
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 529..656
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 265..284
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 656 AA; 73838 MW; CE2F1C8AD4092E4A CRC64;
MDMSQYLDMF LEESYENLQN LNEDILGLEK NPEDKDLINA IFRAAHTLKG MAGSMGFSDI
AELTHKMENV LDKFRNDELK VTSEVITILF RCLDTLEKMI SNIQNGSNEI VDINEIMLQL
QSIVDSKNSD KHVEKKNLDD FKLNEYDINI VKQAYEKGYK VYKVDVELIK DCVLKSARAF
LVYKTLESIG EIVKSSPSIE DIEQEKFDLT FSIVVISDKQ KETIEGMVLA ISEIKKVNVD
LIENVKNEIK ENEDKKDQTA VEKAAAENIK NSKEDEKNTK KTHQSVRVDI ERLDKFMNLV
GELVIHRTRL EQISNNHRLN DLHETLEQVG RITTDLQDLV MKVRMLPIER VFNRFPRMVR
DLAQELNKDI EFIIEGEETE LDRTVIDEIG EPLVHLIRNA VDHGIEPVEE RIKKGKNPKG
VVKLTAYQEG NKAVIRIDDD GNGFNLDKIK KKAQSLGIDT EGMSNNDIKN LIFLQGFSTS
DKVTDISGRG VGMDVVKTKI ASLGGTIDVV SEFGKGSSFI IRLPLTLSII QALLVKVGSE
TLAISLGFID RVINVNINEI KLTNNKEVIM YRGSIIPVVR LADRLNLVES DNSEKYVVIV
KVGEKTVGLI VDSLFGQQEI VIKSMGKTLQ SLKEYVGATI LGDGLVTLIV DVAALV
//
