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Database: UniProt
Entry: E6J9Z2_9ACTN
LinkDB: E6J9Z2_9ACTN
Original site: E6J9Z2_9ACTN 
ID   E6J9Z2_9ACTN            Unreviewed;       575 AA.
AC   E6J9Z2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Sensor histidine kinase MtrB {ECO:0000256|ARBA:ARBA00035305};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ES5_10222 {ECO:0000313|EMBL:EFV91590.1};
OS   Dietzia cinnamea P4.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC   Dietzia.
OX   NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV91590.1, ECO:0000313|Proteomes:UP000004165};
RN   [1] {ECO:0000313|EMBL:EFV91590.1, ECO:0000313|Proteomes:UP000004165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P4 {ECO:0000313|EMBL:EFV91590.1,
RC   ECO:0000313|Proteomes:UP000004165};
RX   PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA   Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA   Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT   "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT   survival in complex tropical soil habitats and biotechnology potential.";
RL   Antonie Van Leeuwenhoek 101:289-302(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFV91590.1}.
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DR   EMBL; AEKG01000213; EFV91590.1; -; Genomic_DNA.
DR   RefSeq; WP_007630484.1; NZ_AEKG01000213.1.
DR   AlphaFoldDB; E6J9Z2; -.
DR   Proteomes; UP000004165; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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:EFV91590.1};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000313|EMBL:EFV91590.1};
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        53..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          252..304
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          319..536
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  61940 MW;  3A63D61CA636F2CA CRC64;
     MTTARPDDAA ASTGDERDTR DAGDANPTLR ERLSSLDPAA LGMRIARMWR RSLQLRVVTS
     TLALSMGVIL TIAFMLQSQM AAQLLSTKLD AAMEQAGRLR LTVEAQIAAT DEGTSEQSRL
     DQARSAISDR GVASGGDSVH AGTFDPILVV PDQTGRGQVV SPAEAEVPPE LQSLVQRGRI
     AYQYVTVDFR GEQAKALMLG TPTDSSIPGL ELYLVYPLIA EEQTLGIMRG IVATAGLAII
     VLSAAIAWIV ARQVVLPVRQ AASIAQRFAN GHLKERMVIR GEDDVARLAM AFNDMAQSLS
     DQITQLEEFG DLQKRFTSDV SHELRTPLTT VRMAADIISD SAEDLDAPTK RAVELLESEL
     DRFESLLTDL LEVSRHDAGM AELSTAELDV RNAVRDAVGT VAHIAEAAGV EVEVDMPDEP
     VMAEVDSRRV ERILRNLVAN ALDHCESKPV RVTLRGSDAA LAVSVRDHGV GLKPGEETRV
     FNRFWRADPS RVRRSGGTGL GLAIALEDAK LHGGRLDCWG SPGEGSCFRL TIPRRRGGTL
     TSSPLPLTPE DEARLVTTGS PTPLERVPGT GEDTP
//
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