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Database: UniProt
Entry: A0A0F2PI71_9FIRM
LinkDB: A0A0F2PI71_9FIRM
Original site: A0A0F2PI71_9FIRM 
ID   A0A0F2PI71_9FIRM        Unreviewed;       438 AA.
AC   A0A0F2PI71;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=VR67_05660 {ECO:0000313|EMBL:KJS13121.1};
OS   Peptococcaceae bacterium BRH_c8a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629715 {ECO:0000313|EMBL:KJS13121.1, ECO:0000313|Proteomes:UP000033493};
RN   [1] {ECO:0000313|EMBL:KJS13121.1, ECO:0000313|Proteomes:UP000033493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c8a {ECO:0000313|EMBL:KJS13121.1};
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 (MAR-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:KJS13121.1}.
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DR   EMBL; LADP01000016; KJS13121.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2PI71; -.
DR   STRING; 1629715.VR67_05660; -.
DR   PATRIC; fig|1629715.3.peg.437; -.
DR   Proteomes; UP000033493; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
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; IPR004358; Sig_transdc_His_kin-like_C.
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; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KJS13121.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:KJS13121.1};
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..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          325..426
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   438 AA;  48757 MW;  01728883D02FF1C1 CRC64;
     MNWKSTTKKL LLLWLVFNIP ALTLVYFWQP ELWYGVSLFI VTGLAPLFIA VVTITDRSGS
     YTSYADEPLD PTLQIANQTL PFLRRGLNEE TASNTAEIIR KIADVAAVAI TDRVRVLAYI
     GAGSDHHKAG GPIMTIATRE VIKTGEMKVI QDNYGLDCPV ADCPLQSAVV VPLKCKGEVM
     GTVKLYRTQQ GDMSPATVKL AVGVAQLLGM QMELAELDRQ AQLVTKAELD ALQAQINPHF
     LFNTLNTIIM FSRTNPETAR RLLIRLASFF RHALKRHGHF NTLKEEIEYF NTYLILERAR
     FRDKLRVVRE IDEELLEYKI PVLTIQPLVE NAIKHGILPK PGQGTVQITV RKHDHEMLIV
     IRDDGVGIDP ALQTKVLTPG FGSGNGVGLS NVHERLKGLF GEEYGLRIVS VPGEGTSIYV
     RIPLVCSTAK KEELVHEA
//
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