ID F6DRL2_DESRL Unreviewed; 483 AA.
AC F6DRL2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Desru_0480 {ECO:0000313|EMBL:AEG58766.1};
OS Desulforamulus ruminis (strain ATCC 23193 / DSM 2154 / NCIMB 8452 / DL)
OS (Desulfotomaculum ruminis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG58766.1, ECO:0000313|Proteomes:UP000009234};
RN [1] {ECO:0000313|Proteomes:UP000009234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC {ECO:0000313|Proteomes:UP000009234};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Mikhailova N., Pagani I., Stams A.J.M., Plugge C.M., Muyzer G.,
RA Kuever J., Parshina S.N., Ivanova A.E., Nazina T.N., Brambilla E.,
RA Spring S., Klenk H.-P., Woyke T.;
RT "Complete sequence of Desulfotomaculum ruminis DSM 2154.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG58766.1, ECO:0000313|Proteomes:UP000009234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC {ECO:0000313|Proteomes:UP000009234};
RX PubMed=23408247; DOI=10.4056/sigs.3226659;
RA Spring S., Visser M., Lu M., Copeland A., Lapidus A., Lucas S., Cheng J.F.,
RA Han C., Tapia R., Goodwin L.A., Pitluck S., Ivanova N., Land M., Hauser L.,
RA Larimer F., Rohde M., Goker M., Detter J.C., Kyrpides N.C., Woyke T.,
RA Schaap P.J., Plugge C.M., Muyzer G., Kuever J., Pereira I.A.,
RA Parshina S.N., Bernier-Latmani R., Stams A.J., Klenk H.P.;
RT "Complete genome sequence of the sulfate-reducing firmicute
RT Desulfotomaculum ruminis type strain (DL(T)).";
RL Stand. Genomic Sci. 7:304-319(2012).
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 ---------------------------------------------------------------------------
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; CP002780; AEG58766.1; -; Genomic_DNA.
DR AlphaFoldDB; F6DRL2; -.
DR STRING; 696281.Desru_0480; -.
DR KEGG; dru:Desru_0480; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_9; -.
DR Proteomes; UP000009234; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 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; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:AEG58766.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000313|EMBL:AEG58766.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009234};
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 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 205..258
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 266..481
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 483 AA; 54872 MW; 7BA75879044FBA45 CRC64;
MLRLFISLCK VIPKALRQLY QWLVKRLYFS ISFKITAVYA VIFGLIFLLF NAGIGVAFVA
YLGRDAQEDL VKDFEIISSL LKDNTELPAR NIEQLSRLDG IEITLFTEKK EVIYTTEETS
PVFYEQKDNR FFVFNTTPTP YGKSTSPLTM VLNDPVIWNS NTVYIQITNP LARETFNVGL
LMAALFSLTM VMIIIVIVIG SRASKKMLLP VAKMTNTVNN ITINALDTRL DVGGSQDELK
DLAKTFNSML DRIQLSYEQQ NQFVSDASHE LRTPIAVIQG YANLLDRWGK NDPSVLEESI
TSIKTESENM KDLIEKLLFL ARGDKATQKI DKESFSIQEL MEEIIKETRL IDPAHEIINW
RNENMIIFAD RKLLKEALRS LIDNSIKYTP KGGKIIIDYF SQKSQAVITI TDTGIGISKE
DLPYIFNRFY RADKSRTKQT GGTGLGLSIA RWIILQHRGT IEVESQINQG TKMTVFLPVQ
NKG
//