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Database: UniProt
Entry: A0A2V2NFH3_9EURY
LinkDB: A0A2V2NFH3_9EURY
Original site: A0A2V2NFH3_9EURY 
ID   A0A2V2NFH3_9EURY        Unreviewed;       804 AA.
AC   A0A2V2NFH3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DK846_02585 {ECO:0000313|EMBL:PWR74063.1};
OS   Methanospirillum lacunae.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=668570 {ECO:0000313|EMBL:PWR74063.1, ECO:0000313|Proteomes:UP000245657};
RN   [1] {ECO:0000313|EMBL:PWR74063.1, ECO:0000313|Proteomes:UP000245657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ki8-1 {ECO:0000313|EMBL:PWR74063.1,
RC   ECO:0000313|Proteomes:UP000245657};
RA   Dueholm M.S., Nielsen P.H., Bakmann L.F., Otzen D.E.;
RT   "Draft genome of Methanospirillum lacunae Ki8-1.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWR74063.1}.
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DR   EMBL; QGMY01000002; PWR74063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V2NFH3; -.
DR   OrthoDB; 293137at2157; -.
DR   Proteomes; UP000245657; Unassembled WGS sequence.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:PWR74063.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245657};
KW   Transferase {ECO:0000313|EMBL:PWR74063.1}.
FT   DOMAIN          5..113
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          334..530
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          532..667
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   DOMAIN          686..802
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          132..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT   MOD_RES         735
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   804 AA;  88218 MW;  C366CF29D22CB0DB CRC64;
     MGLTGEEFLA QLLETFKGEA QEHLQTIASG LIVLEQNSTP VDEYEKVIEQ VFRETHSLKG
     AARAVGLREI ETLCQQQESV FSEVKKGKLI LTPDSFDLFH EVIHAVEQLL IQEKGVKTAD
     LIKRLKSLIT KTSAGPVPTH PSSLVNLSEP GSPPLPTPQI NNSIKPSSQD LYSGLSKEKT
     PQNPNSIAEP EHLNQKEYGT GSKLTSSGEE NLQSPITTKS VSTIKISSDR LETLFARADD
     LMGARLAVSQ RSSSIYNLLQ NFLAWRWAWT QITTDIEHLR TGAEAAGFHQ AEIDHITEFL
     KYNHDFIQVL EKKLTSISRA AARDHYLLDT ATTELIDEIK QVILVPASSL LEIYPRVARD
     LSREYGKLVD ITISGAEIEI DRRILEELKD PILHIIRNSI DHGIESPEIR KEKGKSERGE
     IKIIVSHLRG HQAEIRISDN GRGLEHATIL SNAISKGIIT KEEAGDLLPD QISRLIFRSG
     LSTSKTISNV SGRGLGLAIA LEKTEQIGGS VKVESGPDGT TFVLTLPLSL ATFRGIKVVI
     SHHPFFLPLR SIERVIRIKP ENLKTIENRT VIETDGEPLA VVSLAHILGL QDSGLTGEKP
     LNLLITSAAG IRFCLHVDEI AGTQEIVVKN LGPQLKRVRH FSGASVTGDG IVIPVISCED
     LAATITGMPH LPQPVLIPDE PAGQRSILVV EDSITSRMLL KNILEGAGYH VETAVDGVDA
     LIKLKQTPVD LVVSDVDMPR MNGFVLTEKI RDDPAFVDIP VILVTSLDSR EDREHGITVG
     ASAYIVKSSF DQSNLLEVIS RHIL
//
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