ID A0A0D8IEV0_9CLOT Unreviewed; 916 AA.
AC A0A0D8IEV0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=resE3 {ECO:0000313|EMBL:AKL94145.1};
GN ORFNames=CACET_c06350 {ECO:0000313|EMBL:AKL94145.1}, TZ02_00850
GN {ECO:0000313|EMBL:KJF28507.1};
OS Clostridium aceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL94145.1, ECO:0000313|Proteomes:UP000035704};
RN [1] {ECO:0000313|EMBL:AKL94145.1, ECO:0000313|Proteomes:UP000035704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL94145.1,
RC ECO:0000313|Proteomes:UP000035704};
RA Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium aceticum DSM 1496.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KJF28507.1, ECO:0000313|Proteomes:UP000032372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:KJF28507.1,
RC ECO:0000313|Proteomes:UP000032372};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Clostridium aceticum DSM 1496, a potential
RT butanol broducer through syngas fermentation.";
RL Submitted (FEB-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};
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DR EMBL; CP009687; AKL94145.1; -; Genomic_DNA.
DR EMBL; JYHU01000002; KJF28507.1; -; Genomic_DNA.
DR RefSeq; WP_044823017.1; NZ_JYHU01000002.1.
DR AlphaFoldDB; A0A0D8IEV0; -.
DR STRING; 84022.CACET_c06350; -.
DR KEGG; cace:CACET_c06350; -.
DR PATRIC; fig|84022.5.peg.1454; -.
DR OrthoDB; 9813394at2; -.
DR Proteomes; UP000032372; Unassembled WGS sequence.
DR Proteomes; UP000035704; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AKL94145.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000035704};
KW Transferase {ECO:0000313|EMBL:AKL94145.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 478..530
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 671..891
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 916 AA; 104974 MW; 63279DE35F146885 CRC64;
MNSRLWGDFV RKGILSLEIE EEISKSWKAS KVCNVSCEAP YEEQEMSSSA LEKLLHLHRY
KLATIKKHLD RLNKGFKENT HKTNYGVLLL SKQGYLLHSI NTFSEEEETL LGLKIGTNWG
IDVKGTTAIG LALTDNKAVV VNNCQHYQER YHPYITEAIP IQNSQRELLY ILGMVSSSCE
HSKLLSTLGN ITAKSIENEI IAMKYKDEIK ELKEKSIKQN KLYETQTNLL NYILNHTKEM
IFIMNEKGKY VLLNKASWKF MKENQVYSLE DIYKKLQVCD LEGKRKTSKE DPTLSVFTEN
PIYRCRAMIK KLQGEERYYN IHSIPYCDHH DRRLAIAIIE DVTDYIELQE MKNSFEHKAE
QLETVINTIS DGIAILSPEG DYIMMNPACL KMLPCLEMEQ QDHCNIHDEA AKEKSCSVID
KKSFEILPCL KAKGQNHRKK FGEVVEEKIC NICTIDKNGS AIEVEDYPLV EVLAGKKIKN
QTFVINKNNK MTYIRLSGSP VFDAAGKLSY AVIGINDITK TTKQEIKIKQ QKEFMNSVMD
SISIPIAVVS YPSGVYEYLN SKQLEIFSEV IGKMLTYKQV IGKTTYEILP PEYLHCIEEQ
KETDVVATEK MVSVQLAKGG TRHYQVVCTT LSNKVDEKKQ IVVVGMDVTP QVKLQEETEL
LTKSKEDYFA TISHELRSPI AIIHSAVQMF KSEHYAKQFN DGTRKLISRV EKNTYRLLRL
VNNFLDITRA EAGFMKLNLT NTNIVTYTDF IVESILPIGE KKGIKIDFLY DCNTKTISLD
IEKYERILLN LLSNAFKFTE ENGRIQVYIK EEEKYMKVGV KDTGIGIPQE EIDKIFDRFY
ISENINKREN GGTGIGLSLV KKLMEFMGGK VEVHSKEGAG SEFILLFPKH IEEENLSNEK
EIQLTESAYL ELENIP
//
