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Database: UniProt
Entry: A0A178LSX3_9MYCO
LinkDB: A0A178LSX3_9MYCO
Original site: A0A178LSX3_9MYCO 
ID   A0A178LSX3_9MYCO        Unreviewed;       525 AA.
AC   A0A178LSX3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   10-APR-2019, entry version 19.
DE   SubName: Full=Histidine kinase {ECO:0000313|EMBL:OAN36715.1};
GN   ORFNames=A4X20_05790 {ECO:0000313|EMBL:OAN36715.1};
OS   Mycolicibacterium iranicum.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=912594 {ECO:0000313|EMBL:OAN36715.1, ECO:0000313|Proteomes:UP000078396};
RN   [1] {ECO:0000313|EMBL:OAN36715.1, ECO:0000313|Proteomes:UP000078396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H39 {ECO:0000313|EMBL:OAN36715.1,
RC   ECO:0000313|Proteomes:UP000078396};
RA   Lymperopoulou D., Adams R.I., Lindow S., Coil D.A., Jospin G.,
RA   Eisen J.A.;
RT   "Draft Genome Sequences of Staphylococcus capitis Strain H36, S.
RT   capitis Strain H65, S. cohnii Strain H62, S. hominis Strain H69,
RT   Mycobacterium iranicum Strain H39, Plantibacter sp. Strain H53,
RT   Pseudomonas oryzihabitans Strain H72, and Microbacterium sp. Strain
RT   H83, isolated from residential settings.";
RL   Submitted (APR-2016) 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;
CC         Evidence={ECO:0000256|SAAS:SAAS01126420};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAN36715.1}.
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DR   EMBL; LWCS01000032; OAN36715.1; -; Genomic_DNA.
DR   STRING; 1370125.AUWT01000003_gene4300; -.
DR   EnsemblBacteria; OAN36715; OAN36715; A4X20_05790.
DR   Proteomes; UP000078396; Unassembled WGS sequence.
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; IPR007891; CHASE3.
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; PF05227; CHASE3; 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;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00925949};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000078396};
KW   Kinase {ECO:0000256|SAAS:SAAS01003914, ECO:0000313|EMBL:OAN36715.1};
KW   Membrane {ECO:0000256|SAAS:SAAS00925724, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00925310};
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     20     43       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    196    214       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      217    269       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      298    518       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   COILED      107    127       {ECO:0000256|SAM:Coils}.
FT   COILED      275    295       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   525 AA;  57862 MW;  3947D9E24DF5FE06 CRC64;
     MTRPQRRRRD VAAGLTVQGW QYVVLSVIGF VFLVGGIAVA VLLNRTDQVS TQLIGNIQPA
     RVSAYQLQAA LRDQETAVRG YLITGDPQFL EPYDQGRLTE QQASAEIRIL EQNRPDLLED
     LDRIEQASGA WRENYAEPLI ASVRSGTAEG VETAGLGKRE FDRLRVLFDT QNEHLAQARN
     DGIDELAQIR GWRNGVLISM LISFGATIVI LALLTRRALV RPLGALAASC RRIAGGSFSE
     RIVARGPKDI RGIANDVEFM RQRIVEELDA SRAAAESLDA HAEELRRSNA ELEQFAYVAS
     HDLQEPLRKV ASFCQLLEKR YGDKLDERGV EYIGFAVDGA KRMQVLINDL LTFSRVGRLN
     ATETEVELDS ALDNALGNLS TAVEESGAVI ERPADGLPGV KGDPTLLAML WQNLIGNAVK
     FRRDGVQPRI VIECVPSSDS EEQSWSFSLT DNGIGIAPEF ADKVFIIFQR LHGRDAYSGT
     GIGLALCKKI VEHHGGNIWI DTTYTAGTRF RFTLPVAADH TADII
//
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