FILI_METH6
ID FILI_METH6 Reviewed; 886 AA.
AC E5KK10; G7WMP7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Methanogenesis regulatory histidine kinase FilI {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000305|PubMed:24748383};
DE AltName: Full=Acyl-homoserine-lactone synthase {ECO:0000303|PubMed:24748383};
DE Short=AHL synthase {ECO:0000303|PubMed:24748383};
GN Name=filI {ECO:0000303|PubMed:22237544};
GN OrderedLocusNames=Mhar_0446 {ECO:0000312|EMBL:AET63831.1};
OS Methanosaeta harundinacea (strain 6Ac).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=1110509;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A AHL SYNTHASE, AND
RP INDUCTION.
RC STRAIN=6Ac;
RX PubMed=22237544; DOI=10.1038/ismej.2011.203;
RA Zhang G., Zhang F., Ding G., Li J., Guo X., Zhu J., Zhou L., Cai S.,
RA Liu X., Luo Y., Zhang G., Shi W., Dong X.;
RT "Acyl homoserine lactone-based quorum sensing in a methanogenic archaeon.";
RL ISME J. 6:1336-1344(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6Ac;
RX PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT "The genome characteristics and predicted function of methyl-group
RT oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT spp.";
RL PLoS ONE 7:E36756-E36756(2012).
RN [3]
RP FUNCTION AS A KINASE, CATALYTIC ACTIVITY, INDUCTION, AND
RP AUTOPHOSPHORYLATION.
RC STRAIN=6Ac;
RX PubMed=24748383; DOI=10.1371/journal.pone.0095502;
RA Li J., Zheng X., Guo X., Qi L., Dong X.;
RT "Characterization of an archaeal two-component system that regulates
RT methanogenesis in Methanosaeta harundinacea.";
RL PLoS ONE 9:E95502-E95502(2014).
CC -!- FUNCTION: Member of the two-component regulatory system FilI/FilRs,
CC which is involved in the regulation of methanogenesis.
CC Autophosphorylates and specifically transfers the phosphoryl group to
CC both FilR1 and FilR2. {ECO:0000269|PubMed:24748383}.
CC -!- FUNCTION: Could also catalyze the synthesis of the quorum sensing (QS)
CC signal molecules carboxyl-acyl homoserine lactones (AHLs), which
CC regulate the transition of the cellular morphology from short cells to
CC filaments and of the carbon metabolic flux from biomass formation to
CC methane production. {ECO:0000269|PubMed:22237544}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:24748383};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:24748383};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Transcriptionally regulated by FilR1 (PubMed:24748383).
CC Transcript level increases with cell density (PubMed:22237544).
CC {ECO:0000269|PubMed:22237544, ECO:0000269|PubMed:24748383}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:24748383}.
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DR EMBL; HQ188282; ADQ42400.1; -; Genomic_DNA.
DR EMBL; CP003117; AET63831.1; -; Genomic_DNA.
DR RefSeq; WP_014586016.1; NC_017527.1.
DR AlphaFoldDB; E5KK10; -.
DR STRING; 1110509.Mhar_0446; -.
DR EnsemblBacteria; AET63831; AET63831; Mhar_0446.
DR GeneID; 25395387; -.
DR KEGG; mhi:Mhar_0446; -.
DR PATRIC; fig|1110509.7.peg.498; -.
DR HOGENOM; CLU_009587_1_0_2; -.
DR OMA; DRTARDW; -.
DR OrthoDB; 16486at2157; -.
DR Proteomes; UP000005877; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR007892; CHASE4.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF05228; CHASE4; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Kinase; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..886
FT /note="Methanogenesis regulatory histidine kinase FilI"
FT /id="PRO_0000433370"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 290..344
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 349..419
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 421..473
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 674..886
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 677
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 886 AA; 98306 MW; 75457C4D7B2E838F CRC64;
MTLRRSILAF TGGMILVLAL ICSTFMCHMM MGTLSDLEEA YVHQKVDGTL FYLQEDLSSL
KRAAEDWGHW NDTRDFVIGE NDQYIQDNLN SWTLSGLDVD FMIYYDRSGN LFYSRAFNHA
TGEEVPAPGR LLSLAKDDPL IAHSSPEDGL TGIVSDPEGL LLVSSTTILD SHWKGPISGT
FIVGRRLDGA RAEGLARLSG IDLRMAATAP VGESEGTNSK TSLLIVKEDS DTLIATKTID
DVYGNPTVLL EAQVPREIRS RGLETIRRQV VGIFLASLLF GGLILLFLEL SILMPLATIT
SSVEAIREQE KGQGSRIPTV GPAELATLAE SINEMLDHLE SYNQKLAMSE KRFRTIVDTA
HDCIFIKDPK SRYVLVNPVM ERIFQLPASK MLGERDEVFF SAETAARIRE KDAGVLSGEP
FVGEVSAHTR AGSSMTFHAV KVPLRDDRGQ VTGICGIARD ITDIKEAGVE LLKRDRLLSA
SAAASYSLLV NYDIDQIIID VLQLLGEAVE ADRAYIFENQ TVDGEVLMSQ RYEWTKGEVE
PQINNPVLQS LPYHPDSSTF YEIISRGRPY VGLVKDLPES ERAYLAPQGI VSILIVPIFV
EDRLWGFIGF DDCHRERFWS NGEISVLQVA AGSIGGAFIR SRTRADLVRA KGELQERIGE
VEAKNAEMER FVYTVSHDLR SPLVTIQGFV GFLREDLSAL DGDKIKIDLA MIEEAVLKMD
HLLKDTLSLS RVGRVVNPPE EGSFGEIVHE ALSQASGELR SRGIKVSLAE GWPRVRVDRL
RVQEALTNLL DNSIKYMGDR PHPEIEVGWR PEGEETVFFV RDNGIGMDPD QWEKVFGLFY
KIDPDSEGSG VGLAIVRRII EVHGGRIWIE SEEGRGTCVL FTLPTP
