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Database: UniProt
Entry: L0DGK4_SINAD
LinkDB: L0DGK4_SINAD
Original site: L0DGK4_SINAD 
ID   L0DGK4_SINAD            Unreviewed;       725 AA.
AC   L0DGK4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Sinac_3689 {ECO:0000313|EMBL:AGA27933.1};
OS   Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS   MOB10).
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Singulisphaera.
OX   NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA27933.1, ECO:0000313|Proteomes:UP000010798};
RN   [1] {ECO:0000313|EMBL:AGA27933.1, ECO:0000313|Proteomes:UP000010798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC   {ECO:0000313|Proteomes:UP000010798};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL   Submitted (FEB-2012) 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; CP003364; AGA27933.1; -; Genomic_DNA.
DR   RefSeq; WP_015247072.1; NZ_JH621484.1.
DR   AlphaFoldDB; L0DGK4; -.
DR   STRING; 886293.Sinac_3689; -.
DR   KEGG; saci:Sinac_3689; -.
DR   eggNOG; COG0643; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   HOGENOM; CLU_000650_5_2_0; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000010798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd00731; CheA_reg; 1.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR004105; CheA-like_dim.
DR   InterPro; IPR037006; CheA-like_homodim_sf.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 2.
DR   Pfam; PF02895; H-kinase_dim; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 2.
DR   SMART; SM01231; H-kinase_dim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 2.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50851; CHEW; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AGA27933.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW   Transferase {ECO:0000313|EMBL:AGA27933.1}.
FT   DOMAIN          1..104
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          199..409
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          411..551
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   DOMAIN          575..708
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   MOD_RES         47
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   725 AA;  77765 MW;  581BF9C007F7D8FB CRC64;
     MSDLDGSLGE FLDETYENLG QLDLDFVAIE ANPHDRSNLL GIARTLHTLK GTCGFFGFTK
     LEELAHAGED LLHKLRASAL NPDAAFIGSM LALVDAIRRI LAHIEREGEE GNDDNSALIA
     RLTTQELGAR PRGDGGAPLP KERLGLDETD LREIRAGEPS ISTVRIGIGL LDRLMDMSGE
     LVLARNQLMQ YAATSDDPRL LGSLGRMSQI TTELQGSVMK ARMQPIGTVW DRIPRVVRDL
     AQSCGKRVRI EFEGRGTELD RTILEAIKDP LTHAVRNAVD HGIETPEERQ AVGKRVEGCL
     RLRAAHESGG VQIEICDDGA GIDPERVRRQ ALKHGLLPRE KLDRLGDREL LQLLFLPGFS
     TTERITSVSG RGVGMDVVKA NVERIGGSVE ISSLIGVGTT LVITLPLTLA VIPSLIVGEG
     NDRYAIPQVA IRELVRIEES RAGGEVETFH GAHVFRLRGT LLPLVELGRA LAGPGGRLTS
     GLGALNIAVL QTDGADYGLV VDQFHDIEEI VVKPLGKHLK EVELFSGATI LGDGTLALIL
     DVPGLAREVG IAAKANHRAS NLPASSNSGA GGEAATTLLL FELGGGRRMA VPIDLVARLE
     EKPASAVERA DGQEVLLHDG RLIPLIRPDG APVMTEVAVS GAEVLKIIVC HAGDRWLGLA
     VDAIHDIVRT TLRVHHSERR EGILGAAVIE GRTTDLLDLP GLIRAVDPLF FATPALVPTL
     PMAEA
//
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