ID C8WN67_EGGLE Unreviewed; 926 AA.
AC C8WN67;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Elen_2843 {ECO:0000313|EMBL:ACV56790.1};
OS Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 /
OS KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=479437 {ECO:0000313|EMBL:ACV56790.1, ECO:0000313|Proteomes:UP000001377};
RN [1] {ECO:0000313|EMBL:ACV56790.1, ECO:0000313|Proteomes:UP000001377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 /
RC NCTC 11813 / VPI 0255 / 1899 B {ECO:0000313|Proteomes:UP000001377};
RX PubMed=21304654; DOI=10.4056/sigs.33592;
RA Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Eggerthella lenta type strain (IPP VPI
RT 0255).";
RL Stand. Genomic Sci. 1:174-182(2009).
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; CP001726; ACV56790.1; -; Genomic_DNA.
DR RefSeq; WP_009305206.1; NC_013204.1.
DR AlphaFoldDB; C8WN67; -.
DR STRING; 479437.Elen_2843; -.
DR PaxDb; 479437-Elen_2843; -.
DR GeneID; 69512108; -.
DR KEGG; ele:Elen_2843; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_113_1_11; -.
DR OMA; LWATAFQ; -.
DR OrthoDB; 9806130at2; -.
DR BioCyc; ELEN479437:G1GFY-2865-MONOMER; -.
DR Proteomes; UP000001377; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACV56790.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001377};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 416..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 478..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 686..912
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 926 AA; 101280 MW; 4B80F8ADAB4F14A9 CRC64;
MDYEARRDPD AILRQIVEEE AAEGDTRGKL KIFFGYAAGV GKTYAMLEEA HAVLEKGFDV
VVGYVEPHTR ADTMALVDGL EQISPSTVQH RGISLREFDL DAVLARHPQI VLVDELAHTN
APGCRHRKRY QDVEELLRAG INVFTTVNVQ HLEGLNDKIA AITHVSVAER IPDRIFDQAA
SVELVDIEPD DLIERLEAGK IYLPDRARTA LGNFFSRKNL AALREIALRR MADRLTRKAE
CTEAGARVEA GEDVLVYVTH NTGNVKAIRA AANMAESYHG ALTAVVVESS QSKKFDSDQR
GRLRANIDLA EELGAHVVTL FGDDIAQQLA QYAVTAGATH IVVGNATGGL SVRSLLRESL
VSRLMKLAHG AVVDVVPTKD LPAQYGRLSE ATGFRLTGAD VWRALASVAI ATAIGLAIYS
LGLAGSVVLM LYLIVALLIA TRADGFFYAL FVSMGSVFAY NFFFTIPRFT LHAVGLNYPI
IFAFLLVGTF AASSLAIRMK RQAESTARRA YRMEVLLESS RKLQGARNAD ECFRLAAEQV
IKLLNRPVVM YRLGIDGRLA KPVVHDVPGT LGGDAGACAL ASPEESAVAA WSAANNERAG
ATTDTLADSQ CLYLPIHSKD AVFGVAGIAM DDIDGEEDFG AFEKNLLLAI LDECGQTTEQ
IVFAEDRRRM EMRMEKETLR ANLLRTISHD LRTPLTSISG DADMLLHDRG ALSAQQKEHL
YRDIHDDACW LVTLVENLLS ITRIDNGTLQ LAEQPELVAD VVREALQHVD RRAGRRRVDV
ELEDELLMAD MDARLIVQVI INLVNNAVSY TPADGRIVVS ARRVVEHDRP RVRIAVADEG
PGISEEDRKH IFDMFYNGST GRRGGKSGDF KRGMGLGLSL CRSIVEVHGG TLDVRNVNPH
GSEFSFTLAA VEAGDVVARS TEEARG
//