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Database: UniProt
Entry: E8WYP1_GRATM
LinkDB: E8WYP1_GRATM
Original site: E8WYP1_GRATM 
ID   E8WYP1_GRATM            Unreviewed;       892 AA.
AC   E8WYP1;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Histidine kinase {ECO:0000313|EMBL:ADW67639.1};
GN   OrderedLocusNames=AciX9_0568 {ECO:0000313|EMBL:ADW67639.1};
OS   Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN   [1] {ECO:0000313|Proteomes:UP000000343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA   Haggblom M.M., Woyke T.;
RT   "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002480; ADW67639.1; -; Genomic_DNA.
DR   RefSeq; WP_013578967.1; NC_015064.1.
DR   AlphaFoldDB; E8WYP1; -.
DR   STRING; 1198114.AciX9_0568; -.
DR   PaxDb; 1198114-AciX9_0568; -.
DR   KEGG; acm:AciX9_0568; -.
DR   eggNOG; COG3292; Bacteria.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_28_2_0; -.
DR   Proteomes; UP000000343; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF07494; Reg_prop; 4.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADW67639.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000343};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..892
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003230075"
FT   TRANSMEM        658..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          801..892
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          673..700
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   892 AA;  96625 MW;  1AEAA2DC0F0C5CBD CRC64;
     MPCRVRLVWA SLSLLSCILP RLSAQDLRYL RHQSWSTEEG LPQNSVHAIQ QSADGFLWIA
     TEAGLARFDG YSFKRFDHSN EPAFRSDDIC CLANAPDGSL RIGTSDGLVL LQHGRFIRAK
     ADEPFPAQND QPLHGPAGSI WSSTNTAVTF TSGTNSLTWH AGSDLPGSRI ESLFVDRHGI
     AWVGTNDGLV ILHPGTKAAT SIDALRGNAV LQTYEDHEGN YWIGTETSGL HILRPVAFRT
     EPSLADKALT TVIQATDGAT WIGTRNDGLR RIVNSTTTQP AKLESLTSSV ILSLAPGLDG
     SVWAGTPDGL NHVSQDGTVK KITSAEGLPD DYIQALLTAP DGSLWIGTRH GLVHLHDAVM
     DVLTAANGLG GDLVGTLMLT RQNELWIGTS GGLSHRSTEG KIKNFTSRDG LPQGIVTALA
     EDSAGRLWIA TSAGALASLT QGVIHTVTTQ SLDAPIHAIV PDQHGYLWLR TEHGIQRVLA
     ADLAACAQGQ TCPAQTNTYG LADGLPSEEM IAAGSPAMTM MANGELWSAT RRGAAITDPA
     TLQTSLIPPP VVIERLLVDE APITLDGSSI EIPPGHVRYT LEFAALTFTT PSKVRYRYRL
     EGLDKGWTDA ANKRSATYTN LPGKDYTFRV QAMNSDGLWS PTGAVLTFRV VRPFYKRWWF
     FTLLAALAVL AAIALYRRRL QRLQSRFDAV LQERSRIARE VHDTLAQDFV GVSIQLDIVT
     HLLTSNKTAA ALEQVRQTRT LVTEGLAAAR QSIWKLRANL AQDSLPTRLA EIVKRYTSDQ
     LPIRLKIGGA FRDLDDSTEN EILRIAQEAL SNVQRHADAS EASVDLRYES DMLVLTIQDN
     GTGFDPTRAA RLEGHYGISG MKERTTLLGG SLELASTPGT GTTILLTIPM TA
//
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