ID A0A1B4VA53_9GAMM Unreviewed; 481 AA.
AC A0A1B4VA53;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:BAU48394.1};
GN ORFNames=SVA_1840 {ECO:0000313|EMBL:BAU48394.1};
OS Sulfurifustis variabilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Sulfurifustis.
OX NCBI_TaxID=1675686 {ECO:0000313|EMBL:BAU48394.1, ECO:0000313|Proteomes:UP000218899};
RN [1] {ECO:0000313|EMBL:BAU48394.1, ECO:0000313|Proteomes:UP000218899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skN76 {ECO:0000313|Proteomes:UP000218899};
RA Miura A., Kojima H., Fukui M.;
RT "Complete genome sequence of Sulfurifustis variabilis.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AP014936; BAU48394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B4VA53; -.
DR KEGG; sva:SVA_1840; -.
DR OrthoDB; 9808408at2; -.
DR Proteomes; UP000218899; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_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; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAU48394.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218899};
KW Transferase {ECO:0000313|EMBL:BAU48394.1};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 24..87
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 92..142
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 143..216
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 218..270
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 54155 MW; 34DAE22E02722CB8 CRC64;
MEASRPPRAR SRPKRPPRAS DADQRERLEK FAELSQEALF IHEEGVIHDI NPAAARMVGV
SPKDLIGKHV FTLVAPESLN SAKTQMDIKP TEPYELLLVR RDGTRFWAEL QGRSLSWRGK
TLRVVMARDA TDRKRAEAAL HDSEALFRQL AENIKEVFFV RDLRENRMIY VSPSYEEIWQ
RPRQGLMENP LDFVQSIHPD DRAAVLDTLR RQAPGDLFRR EYRIVRSSGE VRWIRARTFP
IMNAAGEVHR IAGVAEDITD FKQAELARLE HEKAQREALV REVHHRIKNN LQGIIGLLQY
EMGGHPGLRE VIQDTIDQIR SIAVIHGLQS LTPGRDLLLC DVVPAVVSAV CESREPRPQI
ALEADLPRSL KLLEPHAVPI ALVINELVTN AVKHAPAWQA SIEIYLEQQA EGGRFVVRTQ
GARLPAGFDF RTGQGLGTGL HLVKSLLPRE GVTLTITQKD NAVHAELGLL PPVVEPLSQP
D
//
