ID U6EEV6_9EURY Unreviewed; 372 AA.
AC U6EEV6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MBMB1_1794 {ECO:0000313|EMBL:CDG65873.1};
OS Methanobacterium sp. MB1.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=1379702 {ECO:0000313|EMBL:CDG65873.1, ECO:0000313|Proteomes:UP000017867};
RN [1] {ECO:0000313|EMBL:CDG65873.1, ECO:0000313|Proteomes:UP000017867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB1 {ECO:0000313|Proteomes:UP000017867};
RA Maus I., Wibberg D., Stantscheff R., Cibis K., Eikmeyer F.G., Puehler A.,
RA Koenig H., Schlueter A.;
RT "Methanobacterium sp. Mb1.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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; HG425166; CDG65873.1; -; Genomic_DNA.
DR AlphaFoldDB; U6EEV6; -.
DR STRING; 1379702.MBMB1_1794; -.
DR KEGG; meth:MBMB1_1794; -.
DR PATRIC; fig|1379702.4.peg.1774; -.
DR HOGENOM; CLU_743170_0_0_2; -.
DR BioCyc; MSP1379702:MBMB1_RS08725-MONOMER; -.
DR Proteomes; UP000017867; Chromosome.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000017867}.
FT DOMAIN 4..117
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 129..224
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 323..372
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 372 AA; 43479 MW; FAE1E620F3E7866A CRC64;
MTDKILLVEN DGVEAINIRQ TLEKMGHEVV YIASRWEEAV EKISNLKPDL IIIDITAKDD
ISNLDLTTDT KNLDLPFIFL TAHHEGLKLE KTKEVSYDYI IKPYTDTELR YAIELSLFKN
RMEKKLKTTS KVTNAIIESS HDSLFLIDPS GVILKVKDAT KHQSYLNSDE MIGKHLRQFL
PDNVFQNWWC HIEETIKIRD VVEFEDEEDQ KYLHHRIVPL VEEEKVQKLA IFIQEITEPK
SYERELLRTS LQLKKTQELS HMGSWDWDKA TGILNCSEEL HRILGVDETF QPTFENIDAL
IHPDDREMCI KKREELFRRG GTAEQEFRIL RPDGEIIHLK QFIHAFFETN TESVVAFGII
RDLTEISKLA RD
//
