GenomeNet

Database: UniProt
Entry: F0RMB7_DEIPM
LinkDB: F0RMB7_DEIPM
Original site: F0RMB7_DEIPM 
ID   F0RMB7_DEIPM            Unreviewed;       468 AA.
AC   F0RMB7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Deipr_1922 {ECO:0000313|EMBL:ADY27054.1};
OS   Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC
OS   101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY27054.1, ECO:0000313|Proteomes:UP000007718};
RN   [1] {ECO:0000313|Proteomes:UP000007718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC   VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA   Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete sequence of chromosome of Deinococcus proteolyticus DSM
RT   20540.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY27054.1, ECO:0000313|Proteomes:UP000007718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC   VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RX   PubMed=22768367; DOI=10.4056/sigs.2756060;
RA   Copeland A., Zeytun A., Yassawong M., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA   Mavromatis K., Liolios K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA   Rohde M., Sikorski J., Pukall R., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of the orange-red pigmented, radioresistant
RT   Deinococcus proteolyticus type strain (MRP(T)).";
RL   Stand. Genomic Sci. 6:240-250(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; CP002536; ADY27054.1; -; Genomic_DNA.
DR   RefSeq; WP_013615662.1; NC_015161.1.
DR   AlphaFoldDB; F0RMB7; -.
DR   STRING; 693977.Deipr_1922; -.
DR   KEGG; dpt:Deipr_1922; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_89_6_0; -.
DR   OrthoDB; 74171at2; -.
DR   Proteomes; UP000007718; Chromosome.
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; 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:SF5; SENSOR HISTIDINE KINASE TRCS; 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; 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   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADY27054.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007718};
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..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          184..238
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          246..461
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   468 AA;  50401 MW;  91FAB9306DCDB2CC CRC64;
     MRLSLRARLT LWAALATVLA ALLVSGGIYL TVRQLLYLSE KEQLLSSVLI VQSRVEREVD
     RVGGAESLRW MWLDLSQIAG ENVQTQKLEL RLVSQVGGQW FYNQTEHFPA GLQLDLPVNL
     YQIRGQDKMI AVRELRTSGP PLLLSVMTDT GSLGQANKAF RGAFWTLLPL ALLLALVLGW
     TVSGRLLAPV RQLEVAAREV GESGDLRRPL PLTDTGDELG LLARALQGTF GQLAQARERE
     QDFARAAAHD LRSPLAALTA RVQGSLSRPR DAERYRQDLQ EIGTDLERLS ALTTHLLLLS
     RDPSSVSRQP LALHPLAADA VDRARELDEL ADVDLQVAPS GRGLWTEGDP VLLGQAVWNL
     VVNAMRYGAG SPVLVRLEGI GESAVISVQD SGPGVSPEIL AQLGQAFYRP DSSRQGQAAG
     GGHGLGLALA QRAAEVHGGR LELQSAAGQG FTARLVLPAC PAPAAEEG
//
DBGET integrated database retrieval system