ID A0A117SL09_9FIRM Unreviewed; 594 AA.
AC A0A117SL09;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=APF77_19505 {ECO:0000313|EMBL:KUO77328.1};
OS Clostridia bacterium BRH_c25.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO77328.1, ECO:0000313|Proteomes:UP000057710};
RN [1] {ECO:0000313|EMBL:KUO77328.1, ECO:0000313|Proteomes:UP000057710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO77328.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-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};
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:KUO77328.1}.
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DR EMBL; LOES01000015; KUO77328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117SL09; -.
DR STRING; 1734399.APF77_19505; -.
DR Proteomes; UP000057710; 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; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; 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 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 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 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 324..376
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 486..590
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 357..396
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 594 AA; 67526 MW; 54E31CAF95E82E78 CRC64;
MGIIRWAKLK YKNITLSGKL IIAMSIAFFI LFSLVISFNQ YRTINIITKN QSTLSAETLN
IKQQNFITYI NQLESYSLML RNDRTFMQII GLNDIQDYSD LLYVRNVLSN MFYSRKDISE
MKLYLTNMGT YYAISKKYPN MRSHINPDLT EIQEFAEASK WPKFKYVTPS KDDTQSFLKL
YRTIINIETQ KPLAYIEMTV DKSYIEDLAN KNSQSQDIFC LLDSKENLYY TNNPDVIQPE
TLAEILTAKV KGDSGQSSGN FITILNDVEY LFIYSVDNAK GWQLLNMTPT SIVNKTAVET
RNITIIVIVI AMIIAMVAIY MLTTTLLKPL KALAAQMEKA GSGDFGATIH IGSSAEIKHL
ETKFNSMLLK IDELIEKNYI SELKEKTARL KALEAQINPH FLYNTLQMIS TQAIVNNQKD
ISNMVLALSS MLRYSITDND IVPLSSEIKH VKAYLTLQKA RFDERLSYNL DVENNIEDLL
LPKISIMSLV ENSIKHGMET TLDKIEINVN VMLRQGFLVI KVKDSGIGMS EERLEHVIEQ
ISVEGEQSQS IGLSNLAGRL RILYGNSAAL EIESNEDNGT TVEMRIPVNV NMIS
//
