ID A0A0E3V6L0_9BACT Unreviewed; 525 AA.
AC A0A0E3V6L0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:AKD54631.1};
GN ORFNames=SD10_06615 {ECO:0000313|EMBL:AKD54631.1};
OS Spirosoma radiotolerans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD54631.1, ECO:0000313|Proteomes:UP000033054};
RN [1] {ECO:0000313|EMBL:AKD54631.1, ECO:0000313|Proteomes:UP000033054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5A {ECO:0000313|EMBL:AKD54631.1,
RC ECO:0000313|Proteomes:UP000033054};
RX PubMed=24748440; DOI=10.1007/s00284-014-0584-x;
RA Lee J.J., Srinivasan S., Lim S., Joe M., Im S., Bae S.I., Park K.R.,
RA Han J.H., Park S.H., Joo B.M., Park S.J., Kim M.K.;
RT "Spirosoma radiotolerans sp. nov., a gamma-radiation-resistant bacterium
RT isolated from gamma ray-irradiated soil.";
RL Curr. Microbiol. 69:286-291(2014).
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DR EMBL; CP010429; AKD54631.1; -; Genomic_DNA.
DR RefSeq; WP_046376231.1; NZ_CP010429.1.
DR AlphaFoldDB; A0A0E3V6L0; -.
DR STRING; 1379870.SD10_06615; -.
DR KEGG; srd:SD10_06615; -.
DR PATRIC; fig|1379870.5.peg.1439; -.
DR HOGENOM; CLU_039270_0_0_10; -.
DR OrthoDB; 9760839at2; -.
DR Proteomes; UP000033054; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF37; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE UHPB; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AKD54631.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000033054};
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 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 401..517
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 450..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 60038 MW; 64EF8B4FEF93205C CRC64;
MPDTLNDNTK DGSVIPVRFT RLYMTLLIIL AVLLTVGQGL TQWRLRAVQD ELWIIRYSAL
QRHQSQQIVK QVLQLADASE QDHFSENVAA LRQVFPVFER YHLQSRQGKV DNPKVYIVNS
DTVQRLYDAI RPQFDAFRQS AHRLMRLQRF DEIKTPEVQA SIKLMLANEK PFLEEMDGIV
REYTTELRAK LTLLQSIELY LYIFTVAVLI GIGFVIFRPA ARRLKQTFAQ LVEAESQTTA
ANKKLLNANR ILKETRQKLF EATKLQYQQE IDDQKLRTSY LIAGQEEERK RLSRELHDGL
GQMLTAIKLQ IEGLEASLTR AAATEQVGTA PHAKNLKTLK SLVTQTIQET RTISNNLMPS
VLSDFGIIPA IKMLAEQDRS DSFDVTFETN FTSDMPRLNK NVEIMLYRVT QEAVSNAVKH
AKPSHIHIEL YERSTFLQLI VSDDGKGFQV PRKKQENGGL KQKSEINGDI TNPSELRPPS
QGLHNMQERT KLLNGKFKLQ SAFGKGTKIQ VSIPYKTHFA SHDTY
//
