ID A0A0E4A065_9BACT Unreviewed; 611 AA.
AC A0A0E4A065;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SD10_14205 {ECO:0000313|EMBL:AKD58532.1};
OS Spirosoma radiotolerans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD58532.1, ECO:0000313|Proteomes:UP000033054};
RN [1] {ECO:0000313|EMBL:AKD58532.1, ECO:0000313|Proteomes:UP000033054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5A {ECO:0000313|EMBL:AKD58532.1,
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; AKD58532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E4A065; -.
DR STRING; 1379870.SD10_14205; -.
DR KEGG; srd:SD10_14205; -.
DR PATRIC; fig|1379870.5.peg.3089; -.
DR HOGENOM; CLU_000445_114_71_10; -.
DR Proteomes; UP000033054; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
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; PF13426; PAS_9; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 2.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AKD58532.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000033054};
KW Transferase {ECO:0000313|EMBL:AKD58532.1}.
FT DOMAIN 1..36
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 109..182
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 184..236
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 237..292
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 312..364
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 389..605
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 611 AA; 70200 MW; D832493DD37722B7 CRC64;
MDLDGYITYA NPAAATLTQY SVQELANLHV SHLYNPTGDT IKAHYELSLT KKAGHFRTEG
WRTKKDQTYC WCEIIYSCLY NEEKGFLGYS CTLIDRSAQM QEAHQLRQQE DRYRLMVEGV
RDYAIFMLDP EGYILTWNEG AKRIKGYAAS EIIGKHFTTF YTAQDLADEK PVRELAIAIQ
TGKYEEEGWR VKKNGSVFWA NVVITALFND QNQHIGFSKV TRDLTERRQT HEALRQSEEQ
YRSLVEQVSD YGIFMMDEKG RVINWNEGAK RINGYLAAEI IGKYFSIFYP QEAILNGKPA
HELTVALETG KYEEEGWRVR KDGSLFWASI VITAIYNSEG VHIGFSKVTR DLTERKQAEQ
SLRESYDRYR LLTVELQRSN EDLQRFAHVA SHDLKEPARK IKLFSNRLQD EYISMLPEKG
QLFVAKIQQA ADRMLSMIQG ILTYSSLNAL SQLLEIIDLN TLLEQIETDL EVLILDKQAH
IDKQRLPPIE GVPVLIYQLF YNLINNSLKF SKVGEPPLIK IFMASEAAEN FVKITVTDNG
IGFDNQYASK IFETFTRLHA KDAYEGTGLG LALCKKIVER HQGTITVQSV INQGSTFIIT
LPRKQNWPNY I
//
