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Database: UniProt
Entry: F0SQ61_RUBBR
LinkDB: F0SQ61_RUBBR
Original site: F0SQ61_RUBBR 
ID   F0SQ61_RUBBR            Unreviewed;       603 AA.
AC   F0SQ61;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Plabr_3641 {ECO:0000313|EMBL:ADY61238.1};
OS   Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM
OS   15109 / NBRC 103401 / IFAM 1448) (Planctomyces brasiliensis).
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Rubinisphaera.
OX   NCBI_TaxID=756272 {ECO:0000313|EMBL:ADY61238.1, ECO:0000313|Proteomes:UP000006860};
RN   [1] {ECO:0000313|Proteomes:UP000006860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448
RC   {ECO:0000313|Proteomes:UP000006860};
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M.,
RA   Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Planctomyces brasiliensis DSM 5305.";
RL   Submitted (FEB-2011) 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};
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DR   EMBL; CP002546; ADY61238.1; -; Genomic_DNA.
DR   RefSeq; WP_013629957.1; NC_015174.1.
DR   AlphaFoldDB; F0SQ61; -.
DR   STRING; 756272.Plabr_3641; -.
DR   KEGG; pbs:Plabr_3641; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_2_0; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000006860; 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; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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   Gene3D; 3.30.450.20; PAS 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADY61238.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006860};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          188..240
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          252..329
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          373..591
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          232..259
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   603 AA;  67142 MW;  60E93E4E5CE44F37 CRC64;
     MLSSRLFWRI FLTHVLLIVV STVALSMTVS RGYRELIESQ FATETENVAQ SLAEYSREVL
     SRERTPHRGD AFYKLADTRG YRVHVFDDEG NVVASTAASS EFDNLRLNGK LTSNLESSTA
     QQMDSSNSED EMVLVRRIGA PSEVLGYLQL EAPRTSIERQ LARLSGMTGQ VTLAVCFFGV
     LLAGILAARI TQPLEELTRA SQAITIGNLY QTVPVNSSDE LGTLAKTFNT MSRELSTRIN
     ELQQQGQQLR ENSERLATVL GGMVEGVIAV DSKEQILFAN DAAFRMIEFE ARRVIGRPYW
     EVVRNTDVQR VVRDVLAGEY QLQREINLAR SQSRIAFIAS RLPGEPCPGV VLVLHDVTEL
     RRLEKIRSEF VSNVGHELKT PVAAIQACTE TLFAGAIDDP EDAGHFLQQI TDHAERLHKL
     IIDLMELAKI ESEEDAFRRE SIDIGVPIQE AIDEHYSVAQ SKHIELTYKS TIEELPVLAD
     LDGVRTIVNN LLDNALNYTP EGGQVRVEWS QQGDDVLILI SDTGMGIERK HLERIFERFY
     RVDSARSRDA GGTGLGLAIV KHLCQLFSGS IDVTSEPNQG STFSIRFPLH RPTSVKSAEA
     IPS
//
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