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
//