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Database: UniProt
Entry: B8GIL9_METPE
LinkDB: B8GIL9_METPE
Original site: B8GIL9_METPE 
ID   B8GIL9_METPE            Unreviewed;       769 AA.
AC   B8GIL9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=PAS/PAC sensor hybrid histidine kinase {ECO:0000313|EMBL:ACL16832.1};
GN   OrderedLocusNames=Mpal_1518 {ECO:0000313|EMBL:ACL16832.1};
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011 {ECO:0000313|EMBL:ACL16832.1, ECO:0000313|Proteomes:UP000002457};
RN   [1] {ECO:0000313|EMBL:ACL16832.1, ECO:0000313|Proteomes:UP000002457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c
RC   {ECO:0000313|Proteomes:UP000002457};
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:e01280-15(2015).
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DR   EMBL; CP001338; ACL16832.1; -; Genomic_DNA.
DR   RefSeq; WP_012618151.1; NC_011832.1.
DR   AlphaFoldDB; B8GIL9; -.
DR   STRING; 521011.Mpal_1518; -.
DR   GeneID; 7271063; -.
DR   KEGG; mpl:Mpal_1518; -.
DR   eggNOG; arCOG02329; Archaea.
DR   eggNOG; arCOG02386; Archaea.
DR   eggNOG; arCOG02391; Archaea.
DR   HOGENOM; CLU_000445_114_51_2; -.
DR   OrthoDB; 115915at2157; -.
DR   Proteomes; UP000002457; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ACL16832.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002457};
KW   Transferase {ECO:0000313|EMBL:ACL16832.1}.
FT   DOMAIN          7..124
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          214..266
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          267..340
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          344..397
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          410..626
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          645..765
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         59
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         699
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   769 AA;  85741 MW;  9BDEEEA4C0172EA0 CRC64;
     MDPDPIRVLL VEDNPGDARL IREMLVEIHT DRYEVVHVER LEYALLHLNN EKFDTILLDL
     NLPDAYGLST LVKIRAKAPH VPVIVVSGLG DEEMAIHALR EGAYTYLVKG QMSGHLLDRS
     IRYSIERERM EQIVQLQRAR EYAENIVDTI RESLIVLDNR LRIVSANRSF YLDFHVTPEQ
     VEGRFIHDLA DQEWNIPQFL ALLEKILHHS FQYEGLELDH EFPALGRRVM LLNARWVYEE
     RGDTDRILLA MEDITERKRA EEALADEKER LAVTLWNIGE GVIVTDVGGS VGMMNRVAES
     LTGWTASEAV GLPIDQVYQV INEKTRNHCV NPVAAVLKKE ETTDSSHFRL LIGKDGIERP
     LGDSVAAVRD KDGKIIGVVI VFRDITAARR MEEDLAKNER LESIGVLAGG IAHDFNNALT
     AIEGNIVVAK AHLKPEEKAY ERLSEAEMAA HRARDLTRQL LTFSRGGKPI KRQLRLNDLL
     IDAVSFALSG SAVRKKFSIA EDLWPVEADE GQIRQVINNL VINADQAMPD GGILDVIGDN
     VSLASDQVLS LKAGNYVRIA VKDHGIGIPK EFLSKIYEPY FTTKQKGSGL GLTVAYSILR
     NHGGSLIVDS VTGGGSTFTL YIPASQMQLP VESVPSVHPL QGNERILWMD DETMIREVGG
     EMLSLLGYRF AFAEEGDQAI ELYKAALESE SPFDAVILDL TGAGGLGGKE TIKQLLELDP
     QVRAIVCSGY SNDPVMANHR EYGFRGVLTK PFTMKELDDQ IHLVIGTEE
//
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