ID E1RF62_METP4 Unreviewed; 955 AA.
AC E1RF62;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mpet_2562 {ECO:0000313|EMBL:ADN37306.1};
OS Methanolacinia petrolearia (strain DSM 11571 / OCM 486 / SEBR 4847)
OS (Methanoplanus petrolearius).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanolacinia.
OX NCBI_TaxID=679926 {ECO:0000313|EMBL:ADN37306.1, ECO:0000313|Proteomes:UP000006565};
RN [1] {ECO:0000313|EMBL:ADN37306.1, ECO:0000313|Proteomes:UP000006565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11571 / OCM 486 / SEBR 4847
RC {ECO:0000313|Proteomes:UP000006565};
RX PubMed=21304750;
RA Brambilla E., Djao O.D., Daligault H., Lapidus A., Lucas S., Hammon N.,
RA Nolan M., Tice H., Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Spring S., Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Methanoplanus petrolearius type strain (SEBR
RT 4847).";
RL Stand. Genomic Sci. 3:203-211(2010).
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; CP002117; ADN37306.1; -; Genomic_DNA.
DR AlphaFoldDB; E1RF62; -.
DR STRING; 679926.Mpet_2562; -.
DR KEGG; mpi:Mpet_2562; -.
DR eggNOG; arCOG02385; Archaea.
DR eggNOG; arCOG06192; Archaea.
DR eggNOG; arCOG06193; Archaea.
DR eggNOG; arCOG06712; Archaea.
DR HOGENOM; CLU_000445_114_58_2; -.
DR OrthoDB; 230688at2157; -.
DR Proteomes; UP000006565; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ADN37306.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000006565};
KW Transferase {ECO:0000313|EMBL:ADN37306.1}.
FT DOMAIN 3..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 134..203
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 207..257
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 314..370
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 386..438
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 439..509
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 528..579
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 615..672
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 848..948
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 241..310
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 955 AA; 108637 MW; 995F96AFD5BBF05C CRC64;
MIKILYVDDE PVLLELARIF IEKSGDFSVD TAESAALALE LMKTGEYDAV ISDYQMAGMD
GIDLLKAIRA SGDKIPFIIF TGKGREEVVI QAFENGADFY IQKGGEPNSQ FVELVHKVRQ
SIALRQTEAA LKDSEEKYRL LVEKANEAIF IAQDHQVRFS NPRFSSIIDI PPGEMVGKSI
DDLIHPDDRE MVLGRYERRI TGKSAPEEYE FRVLDSSGNT HWVKIHATPI HWEERPALLI
ILDEITERKA AEDELQESNQ KLAELNEELR MHLNTIEERN DEIQGAYEQL KAAEEELRQN
YNELGQKEIL LRESEEKFRR IVETAEEGIW EMDNREMTTF VNKKMAEMLG YSTKEMVGRK
ISSFIHDEDQ KDHLSEIEHR KGGESGLYVR RMMRKDGEIR WMKVKSTHVF GKSGNFRGSF
AMVSDITEQK YAEDALRESR QDLMDIIDFL PDATFVIDNH GRVIAWNRAI EEMTGVRSED
IVGRGNYEYA LPFYRERKPI LIDMVLENDF LGESHYPSVI TDGNRLVSEI EIPYLYGGKG
AYLWFIATPL YDSSGKITGA IESIRDITAK REFEETLVNR NKELTSAYEQ LAVMEEELRQ
GYDELEKGHT ELRESEEKYR NLIENAPIGI FTSTSDGEFL TLNGTGAKIL GFSSPEEVTG
NPGSLKEILH SDPAGSDLLT DILLEKGYLE DFNFEYIKKG ETKKKHLKIN ACISQSNKDG
SFIVLGFFDD VGDVKNIRET LENANHKLKL LYSITRHDIL NSVMAAYCFI ELLKNPEDPE
YGQYIETLHE LLEKIQKQIE FTREYENLGS HVPVWQNLAE ILAVVRSQSS LPFEIVGCDI
EILADPILRK VFDTLLDNTV RHGGGSVSRV EVSCMRSENG GYSIVWKDDG TGIPDDDKEL
IFERGFGKNT GLGLFLAREI LAISGVEIKE CGSPGKGARF EMTVPEGKYR VIYGC
//
