ID Q47LZ4_THEFY Unreviewed; 579 AA.
AC Q47LZ4;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Sensor histidine kinase MtrB {ECO:0000256|ARBA:ARBA00035305};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Tfu_2495 {ECO:0000313|EMBL:AAZ56528.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ56528.1};
RN [1] {ECO:0000313|EMBL:AAZ56528.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ56528.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000088; AAZ56528.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47LZ4; -.
DR STRING; 269800.Tfu_2495; -.
DR KEGG; tfu:Tfu_2495; -.
DR eggNOG; COG3850; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_18_11; -.
DR OrthoDB; 9786919at2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR047669; MtrAB_MtrB.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; NF040691; MtrAB_MtrB; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:AAZ56528.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAZ56528.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000313|EMBL:AAZ56528.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 251..303
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 318..535
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 579 AA; 63013 MW; 182F34FD6E17C043 CRC64;
MTDSVQAPSP NAAAPALEGE AAFTRWQRMG NALRAGYVVT QRLARGLVTA VHSRWRRSLQ
LRVVTTTLMA SVLVTAILGF FMVQQVRSDL LKAKEQAAFS DHHMGLTAAL GILQDSGQQD
PERQLDEIVE ELSARSGATG LYDVVILPSV GGMTGRASGG VGEASIPAQL REEVQNSNGD
TQHGRYTEII RGPNREPGLA VGAQLSSAYE LYYLFPLDHE QQMLDLVQRT LALVASVMVL
LLAAIAYVVT RQVVTPVRQA ASSAEKLSSG DLSERMEVRG EDDLARLAVS FNDMAGSLQE
KIQELEELSK VQRQFVSDVS HELRTPLTTI RMAGDLLFEE RDSFDPTVRR SVELLQSQLE
RFEELLNDLL EISRHDAGAA TLALERADIR DSVLQAVREA EQIAEKRGIK VILRLPTEPC
TAEFDSRRIN RILRNLIVNA IEHSEGKDVI VTAAADRDAV AVAVRDFGVG LKEGEEHLCF
DRFWRADPAR ARTTGGTGLG LAIAKEDAQL HGGWLQAWGR PGKGAQFRLS LPRVAGTELR
GSPLPLVPPE MALGGNLSVL SGQQVDLETG RGTSAGEEA
//
