ID D9SQU7_CLOC7 Unreviewed; 598 AA.
AC D9SQU7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Clocel_2593 {ECO:0000313|EMBL:ADL52303.1};
OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL52303.1, ECO:0000313|Proteomes:UP000002730};
RN [1] {ECO:0000313|EMBL:ADL52303.1, ECO:0000313|Proteomes:UP000002730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC {ECO:0000313|Proteomes:UP000002730};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Clostridium cellulovorans 743B.";
RL Submitted (AUG-2010) 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002160; ADL52303.1; -; Genomic_DNA.
DR AlphaFoldDB; D9SQU7; -.
DR STRING; 573061.Clocel_2593; -.
DR KEGG; ccb:Clocel_2593; -.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_020473_6_1_9; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000002730; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADL52303.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002730};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..387
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 494..596
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 598 AA; 69008 MW; E9CED9EAE3822549 CRC64;
MICRLNIFKL RDIFTSLKNK YLNLKISLKI IIYFSVIFII ATLVLNFTYG KINRTYMTEK
IKQGSFEALE STKASINLII DNVSNASKMI VSSDDVQNSL KNTNLKSDLE AQNNINKYLS
QFTNFNPYIA SIYILDNYSN KYYSENNTYK SFTVDQIRNM EWYNEVLNEN GGYILKLNGG
GLFHNKTGNY ESYVSFIRII NDINTQEKVG VLIININENA FYDYIVKVSN QYGTKLIIEN
ENGEVITKPD IEENILKVAE NEKYSAKNKG FVIKNLNYKD YIISNIKMEK YDWNLISISE
YSQLSEQSKY TKNFMVVFIS ISLLLIVFGA IGISNMITKP LTKLHKSMKD VKNGEFKIVE
GKTYNDEVGE LKKVYNIMVQ NIQFLLDKIR EDELFKRKAE LDLLMSQIKP HFLYNTFDSI
SSLALSGENK RVYQIVKALG TFYRTSLSNG RDVITIEEEI NTIKSYLVIQ NIRYNDKFDV
QYNLDPNCNE FKIIKLVLQP LVENSIYHGL RSKVEKGMIK ISTYEEGEKI VLSVEDNGCG
IDESKIKELM DGRTSGIGVR ATKERLRVFY GAKSEFIIKS EKDVGTKIII KIHKKEVN
//