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Database: UniProt
Entry: A0A3R6UB12_9FIRM
LinkDB: A0A3R6UB12_9FIRM
Original site: A0A3R6UB12_9FIRM 
ID   A0A3R6UB12_9FIRM        Unreviewed;       397 AA.
AC   A0A3R6UB12;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DXB15_15185 {ECO:0000313|EMBL:RHV64812.1};
OS   Roseburia sp. OM02-15.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=2292368 {ECO:0000313|EMBL:RHV64812.1, ECO:0000313|Proteomes:UP000285983};
RN   [1] {ECO:0000313|EMBL:RHV64812.1, ECO:0000313|Proteomes:UP000285983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OM02-15 {ECO:0000313|EMBL:RHV64812.1,
RC   ECO:0000313|Proteomes:UP000285983};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-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:RHV64812.1}.
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DR   EMBL; QULX01000026; RHV64812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R6UB12; -.
DR   Proteomes; UP000285983; 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   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RHV64812.1};
KW   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        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          109..162
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          170..384
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   397 AA;  45285 MW;  4F2A68A76813FDA4 CRC64;
     MKKMSLQWRL TCIITLYIAV ICGCLTMFVY KNGVYYIDSL QETVDAREDD NENDSDEIYI
     SIPEDKWDEF ANDFSLQVYS NKADYKRNSF IISAVLALMG GVVTYFISGH ALRPIREFSD
     KIEEVEAQNL ADSRIEENKV KELNQLSISY NRMLTRLSDA FEVQRQFTAN AAHELRTPLS
     LIQVQLDLYN AARHPGNDAD TMQTIKMVTE QNDRLNKMVK TLLDMSELQT VGRDEVIAVD
     ALVDEVLADL EPLAQEKNIT LVENCKNITM RGSDILIYRM VYNLVENAIK YNHVDGQVIV
     TAYQEENHVH LSVEDTGSGI PEELKERVFE PFFRVDKSRS RELGGVGLGL ALVREIVRVH
     DGSITVRSNP SGGTVFELQF MHHMYSNIDK SPTLRYS
//
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