ID A0A3E2NH46_9CLOT Unreviewed; 474 AA.
AC A0A3E2NH46;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DS742_04510 {ECO:0000313|EMBL:RFZ80263.1};
OS Clostridium indicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=759821 {ECO:0000313|EMBL:RFZ80263.1, ECO:0000313|Proteomes:UP000260680};
RN [1] {ECO:0000313|EMBL:RFZ80263.1, ECO:0000313|Proteomes:UP000260680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PI-S10-A1B {ECO:0000313|EMBL:RFZ80263.1,
RC ECO:0000313|Proteomes:UP000260680};
RA Krishna G., Summeta K., Shikha S., Prabhu P.B., Suresh K.;
RT "New species, Clostridium PI-S10-A1B.";
RL Submitted (JUL-2018) 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 -!- 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:RFZ80263.1}.
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DR EMBL; QOHO01000013; RFZ80263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2NH46; -.
DR OrthoDB; 1410840at2; -.
DR Proteomes; UP000260680; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; 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:SF9; HISTIDINE KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000260680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..243
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 371..474
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 248..275
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 474 AA; 54734 MW; 4317040B112BAFD5 CRC64;
MVILIVALSI IFNIVILDFA LNGFNQILED NSRCHDYQAA MEDETRAFKN YVKDRSQESR
ELFDTACART EHSVSQLPFD YDKVGTERYS ITWSIRNGYE NYSKWRDLFL MGKDENGFSI
TQYINELYRI YRMQDYLSDY GKRLVQSTLR EGTDAYYARV PILYRFPVVI LVLAVFSISG
TFYVSRMMNR DMVDPVVRLA CISRKIAGND FSNEDVVIDN QDEIGELVRA FNKMKHSTSQ
YITTLKEKNE MADLLHKEEI EKMEIEKRLD ATKLELLKNQ INPHFLFNTL NMISCMAKLE
DAGTTERMTE CLGNLFRYNL KTPESEVLLK KELQVVSDYM YLQQMRFGSR LHYDIQCLVD
STRIMIPTFT LQPLVENAVV HGISKKEEGG SIRIRIWEKN QKIIISVADT GVGMSEESLA
ELREALAVHS TARVGIGAGN IYQRIHRMYD GGDFQIYSRQ GHGTAVLLTI PVRL
//