ID A0A221NXR3_9ACTN Unreviewed; 704 AA.
AC A0A221NXR3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Sensor histidine kinase MtrB {ECO:0000256|ARBA:ARBA00035305};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LK07_12865 {ECO:0000313|EMBL:ASN24779.1};
OS Streptomyces pluripotens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1355015 {ECO:0000313|EMBL:ASN24779.1, ECO:0000313|Proteomes:UP000031501};
RN [1] {ECO:0000313|EMBL:ASN24779.1, ECO:0000313|Proteomes:UP000031501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 137 {ECO:0000313|EMBL:ASN24779.1,
RC ECO:0000313|Proteomes:UP000031501};
RA Ser H.-L., Lee L.-H.;
RT "Genome sequence of Streptomyces pluripotens MUSC 137T.";
RL Submitted (JUL-2017) 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; CP022433; ASN24779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221NXR3; -.
DR STRING; 1355015.LK06_011735; -.
DR KEGG; splu:LK06_011735; -.
DR OrthoDB; 9786919at2; -.
DR Proteomes; UP000031501; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ASN24779.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031501};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 71..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 295..347
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 362..579
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 74268 MW; 024FC5E560F4CB77 CRC64;
MSGDSAASAP GRSGARPGRP VGRASAGARF SRLFEGGLLQ GGVQGSPVLR LFLRWVRRPL
LPVMRLWRRN IQLKVVATTL LMSLGVVLLL GFVVIGQVRN GLLDAKVRAS QSQATGGFAV
ARTKADEAAG GAGNGGATAA TGTGDTTSTA DGRQSQNVIQ WMSDLVESLS SGGAGAFDVV
TLPVGDDSGG GRSPRGSGNV DPTSSVPADL RERVNSGTTA AQSYTRIVYY NGKESQPGLV
IGKQVNDPNG HPYELYYLFP FTQEEKSLSL VKGTLATAGL FVVVLLGAIA WLVVRQVVTP
VRMAAGIAER LSAGRLQERM KVTGEDDIAR LGEAFNKMAQ NLQLQIQQLE DLSRMQRRFV
SDVSHELRTP LTTVRMAADV IHEAREDFDP VTARSAELLA DQLDRFESLL GDLLEISRFD
AGAAALEAEP IDLREVVRRV VTGAEPLAER KGTHIRVTGD QQPVVAEADA RRVERVLRNL
VVNAVEHGEG KDVIVKLAAA GGAVAVAVRD YGVGLKPGEA TRVFSRFWRA DPARARTTGG
TGLGLSIALE DARLHGGWLQ AWGEPGGGSQ FRLTLPRTAD EPLRGSPIPL EPRDSRRNQG
LDETGRPGGA GEKKATVPVQ QAAAQRPSLP PRAPISPRLA SVTPAADPTA LPGNGIGARV
VPRPAGGALH HDQPAEDPVP GTGAAGQESS TEDATEPGEA FRGR
//
