ID D5EA23_METMS Unreviewed; 755 AA.
AC D5EA23;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Signal transduction histidine kinase {ECO:0000313|EMBL:ADE36024.1};
DE Flags: Precursor;
GN OrderedLocusNames=Mmah_0496 {ECO:0000313|EMBL:ADE36024.1};
OS Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE36024.1, ECO:0000313|Proteomes:UP000001059};
RN [1] {ECO:0000313|EMBL:ADE36024.1, ECO:0000313|Proteomes:UP000001059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35705 / DSM 5219 / SLP
RC {ECO:0000313|Proteomes:UP000001059};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Methanohalophilus mahii DSM 5219.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001994; ADE36024.1; -; Genomic_DNA.
DR AlphaFoldDB; D5EA23; -.
DR STRING; 547558.Mmah_0496; -.
DR KEGG; mmh:Mmah_0496; -.
DR HOGENOM; CLU_013348_0_0_2; -.
DR Proteomes; UP000001059; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 1.
DR CDD; cd12913; PDC1_MCP_like; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:ADE36024.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW Transferase {ECO:0000313|EMBL:ADE36024.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 469..545
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 553..745
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 755 AA; 85596 MW; 74BC492204C0EFE5 CRC64;
MIEMTWKDVP LKSKLMFFIL MGILVVLITS TAVIISTVTT QEEDLAYQQS IQKAKNYANQ
FDIEMRSNQA TGQAIAHSLS QYHSENRTEV NNILLKLLEE NPDLLGTYVC FEPNAFDGMD
SRYVNTTGHD ETGRFIPYWN RIPGNITLDP LLDYDTSVYY QLPKEIKKDI VTEPYYYEGV
FIVSYVTPVM RGGEFIGIGG VDVSLNHLNG VVNNVKAFDT GYAIMTGNTG ILISHPTNEE
LVGAKTLYDY GVPEITRMAD EIKLGKSGYI ETIDPITGKD VVMFYEPIKT SKFAFILVVP
KDEMLAGVTD LRNRLLLISS ISLIFMGAIA ILITRSVTGP INEIVNDFKN ISDAAIGGKL
DERAETDVDI DFREIPEGLN DILNALENAS QLREEMEKVV NNSPVIVFKW KAEKNWPVEF
VSKNISQFGY SPEDFGPNGL DYGDIIHPDD LPGVETKLGE ICSGKETQFN IEYRILTKDG
ETRWVDERTF IQRNQREIIH NMINKDNDID SQVSDLKGKC HDVKYLQGVI VNIDERKQAE
EALLKIEDIR KKEIHHRIKN NLQVISTLLY LESEKFKDDD VLDAFNNSRD RVRTMALVHE
KLYQSKDMES IDFSDYSKNL INYLSQSYVL EKSEVDIKIN VENIFLGMDT AVPLGIIINE
LVSNSLKYAF DKGKGTIIVE LRKINDHHKL VVSDNGIGMK DEIDFEDTDS LGLLLVHTLA
EQINATIEID TSKGTKFEIT FQEKNQELRE GEDVR
//
