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Database: UniProt
Entry: A0A0E3V8Y1_9BACT
LinkDB: A0A0E3V8Y1_9BACT
Original site: A0A0E3V8Y1_9BACT 
ID   A0A0E3V8Y1_9BACT        Unreviewed;       556 AA.
AC   A0A0E3V8Y1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SD10_22090 {ECO:0000313|EMBL:AKD57182.1};
OS   Spirosoma radiotolerans.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD57182.1, ECO:0000313|Proteomes:UP000033054};
RN   [1] {ECO:0000313|EMBL:AKD57182.1, ECO:0000313|Proteomes:UP000033054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG5A {ECO:0000313|EMBL:AKD57182.1,
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).
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; CP010429; AKD57182.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3V8Y1; -.
DR   STRING; 1379870.SD10_22090; -.
DR   KEGG; srd:SD10_22090; -.
DR   PATRIC; fig|1379870.5.peg.4784; -.
DR   HOGENOM; CLU_000445_114_71_10; -.
DR   OrthoDB; 9766459at2; -.
DR   Proteomes; UP000033054; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 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; 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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033054};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          166..236
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          239..292
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          330..556
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          146..176
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          286..313
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   556 AA;  62442 MW;  63EF17FB5EB62E7C CRC64;
     MHELTKLMLD NEMDLILVHK RSMKLAELAG LSLAAQTTFA TAVSEVARLA VISGEQASLR
     LGVKSNDTKG WRIFAYLHDR REYSAGTFEA ALAHARRLVD DLSIQVNGKG TEIQLYCAVQ
     DSKSVNSDRI HGWKKTFLRE PPASPYDDIK RKNSQLQELA ERLGQSEQQY KQVTNSLPLL
     IFSMTSTGRL TYVNQGFTNF LGKSMEELNE ESWLRHFHDE DYIDLTRIWA DSIAAGLPFK
     GEGRLRNRLT GSYVWHLVSA TPLRDASQEV IHWTGFLADI DVQKGIEQTL RDNEELRQNK
     SQLETSQQQL ADDIGELSRS NTELSQFAYV ASHDLQEPLR KIQAFSSMLT EQYGPALDSN
     AQDIIRRMQM ATGRMQELIR GLLAYSRLNT EKHSFHVVSL SALVAEVQGD LETAIRDRNA
     QIQVDALPVI QGNTLQLRQL FQNLLSNALK FTPSDRSPIV RVNTRTVPAD QLPIPIAGKS
     TSYLEVSVVD NGIGFDDKYV DRIFNLFQRL HGRSEYAGTG IGLAICKKVV DNHGGYLTAR
     SQPGKGATFL VYLPMN
//
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