ID E6W4D3_DESIS Unreviewed; 662 AA.
AC E6W4D3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Selin_1172 {ECO:0000313|EMBL:ADU65907.1};
OS Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC Desulfurispirillum.
OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU65907.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU65907.1, ECO:0000313|Proteomes:UP000002572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC {ECO:0000313|Proteomes:UP000002572};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA Bini E., Woyke T.;
RT "Complete sequence of Desulfurispirillum indicum S5.";
RL Submitted (DEC-2010) 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; CP002432; ADU65907.1; -; Genomic_DNA.
DR AlphaFoldDB; E6W4D3; -.
DR STRING; 653733.Selin_1172; -.
DR KEGG; din:Selin_1172; -.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_000445_114_69_0; -.
DR InParanoid; E6W4D3; -.
DR Proteomes; UP000002572; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd13704; PBP2_HisK; 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 Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 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; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 251..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..349
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 449..662
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 662 AA; 75928 MW; 9F75AA0861C526A2 CRC64;
MRCLYVFVLM AFFVGTSFGE PRHEYAHQTL IVAYEPDLAP LNAAQEGVPA GFAIEVLDRI
AALHHIRLQY VPMARSRAIE AIREQQVDII VSIPFSRSYA ELMDFSEPFY STSVGILTPA
DRHGIDAVTD LSETLVALQS HTIEYDFLKN IRRIHYQVAG SQRAAIEAFL LGRADVFVGD
VAIAEHYLEQ HHLEDRYSFA RTYLMPLDYS FAVSKDNYRL LHTLNSGIRH VKSTGEYGDM
YQKWFKTPQE FASGTLLVVV KITLALIAVF LILFLVGARW NRQLKKEVDR KTRDLSHLNA
SLVEQVELTR NNVEFLRQII DSSPRGIVTL NREGLITKFN QKASVIVGLR ELPLGEHYSR
VQLISELLKN KADEVLSGRK NYYLGETKEW ERDPETLYQL RYYVYPLFSF EQHINGLILT
FEDVTEETEL RKKLFEQEKS KALSRVVAGI AHEIRNPLSS IKTFVELIPT KLHNERFQKE
ISTYVPREIT RVNQLIEGLI NYARPRQQIF ETIAASTILD ECYILFERSV MNKGFALLRD
YQSHRQICVD HNQIKQVVIN FLINALDALE EKRLKSDEPL HITLRTRDKA DRVCIQIVDD
GIGMDEDGRV KALEPFFTTK PKGTGLGIPI ADQLIKENRG ELHISSNQKF GTVISVYFDS
AL
//
