(data stored in ACNUC7421 zone)

SWISSPROT: Q47TC3_THEFY

ID   Q47TC3_THEFY            Unreviewed;       474 AA.
AC   Q47TC3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 105.
DE   SubName: Full=Signal transduction histidine kinase {ECO:0000313|EMBL:AAZ54294.1};
GN   OrderedLocusNames=Tfu_0256 {ECO:0000313|EMBL:AAZ54294.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54294.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC         Evidence={ECO:0000256|SAAS:SAAS01126420};
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DR   EMBL; CP000088; AAZ54294.1; -; Genomic_DNA.
DR   RefSeq; WP_011290703.1; NC_007333.1.
DR   STRING; 269800.Tfu_0256; -.
DR   EnsemblBacteria; AAZ54294; AAZ54294; Tfu_0256.
DR   KEGG; tfu:Tfu_0256; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; ENOG410XNMH; LUCA.
DR   HOGENOM; HOG000223177; -.
DR   KO; K02484; -.
DR   OMA; DEREDYP; -.
DR   OrthoDB; 692375at2; -.
DR   BioCyc; TFUS269800:G1G4Q-260-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0016021; C:integral component of 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_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 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; IPR004358; Sig_transdc_His_kin-like_C.
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; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
DR   PRODOM; Q47TC3.
DR   SWISS-2DPAGE; Q47TC3.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00925949};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Kinase {ECO:0000256|SAAS:SAAS01003914, ECO:0000313|EMBL:AAZ54294.1};
KW   Membrane {ECO:0000256|SAAS:SAAS00925724, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00925310};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|SAAS:SAAS01003669};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00926038,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00926160,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|SAAS:SAAS00924981}.
FT   TRANSMEM     17     40       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    167    191       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      191    245       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      260    470       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
SQ   SEQUENCE   474 AA;  51537 MW;  431D124C97FAC29A CRC64;
     MIIGGLFAPP GTLRSRLLAG LLIVTGVGLL VSSLVSVLTL RSFITERLEA QLLFTTERAM
     IRLDNDTPPV GVDAPSPSPY FVVLLNPETG EVNQIYGDTL REDVVLNRLA HLSLTELRSY
     ASSQEIVELD TPDERVPPHL ITVRMRPNAI MVSGVPTDER EDYPRQLVTV QLITAVLLLG
     GLLLIGGRLI VRALAPLDRM ATTAGQISTG SDLGDRMPDA DPYSEVGRLG MAINTMLARL
     ENAFRAKAES ERRVRDFAAD ASHELRTPLT TILGYAELYR QGAIPDAELP EAMRRVEAEA
     TRMSKLVGEL LELARLDRTG SLELATRDVA EIVRDMTGDA ASLEPEREFT LDVPDRLFWR
     IDETRFRQIL ANLLSNVREH TPPDTPVTVR LHSDGDEVVL SVTDAGPGMS PEDASRVFDR
     FYRAARDPGG GSGLGLPIVK AIADAHGGSV TLDTRPGEGT TVTVCIPSGD HSTD
//

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