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Database: UniProt
Entry: B1W4D8_STRGG
LinkDB: B1W4D8_STRGG
Original site: B1W4D8_STRGG 
ID   B1W4D8_STRGG            Unreviewed;      1002 AA.
AC   B1W4D8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=SGR_6126 {ECO:0000313|EMBL:BAG22955.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG22955.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG22955.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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};
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DR   EMBL; AP009493; BAG22955.1; -; Genomic_DNA.
DR   RefSeq; WP_012381727.1; NC_010572.1.
DR   AlphaFoldDB; B1W4D8; -.
DR   GeneID; 6212910; -.
DR   KEGG; sgr:SGR_6126; -.
DR   PATRIC; fig|455632.4.peg.6282; -.
DR   eggNOG; COG0642; Bacteria.
DR   HOGENOM; CLU_002554_2_0_11; -.
DR   OMA; NTRDWPI; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR013587; Nitrate/nitrite_sensing.
DR   InterPro; IPR010910; Nitrate/nitrite_sensing_bac.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08376; NIT; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50906; NIT; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAG22955.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          53..305
FT                   /note="NIT"
FT                   /evidence="ECO:0000259|PROSITE:PS50906"
FT   DOMAIN          522..627
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          649..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..787
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        808..825
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..883
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..953
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1002 AA;  109411 MW;  5D4F6934341EF9FD CRC64;
     MRFRGKSIRR KIVALLLVPL VSLTGLWVFA TYITGRQADE LMSAGSIVEK VGHPLEDAVR
     AVQDERRQTL VFLADPRASD ALPVLMGQRA ATDRIVGEVR ENAREQDVRD ALSVSDESRL
     DAILSAVDGL DALRASVEKR TIGRAKALDF YNGLIDPSYR FLTGLHTLEN VSMDKQMRAL
     VGVSRAREML SREDAMVASG LIAGRFTTAE LRRISGLVAQ RELLYEVSLD NLPAAERRRV
     EQFWASPETE PLRTAEDALI AAGPAKRPDA VDADRWEQSA VPVLDRLAGD ATEMGNRFQD
     RAEPAAYRVL AQAGIAGVLG FLALIVSVFV SVRIGRQLVR DLSRLRKDAH EVSGVRLPSV
     MRRLAAGEQV DVETEAPHLS YEPDEIGQVG QALNTLQRAA VEAAVKQADM RRGVSEVFVN
     LARRNQVLLH RQLTLLDAME RRTENGDELA DLFRLDHLTT RMRRHAEGLV ILSGAAPSRQ
     WRKPIQLMDV VRAAVAEVED YERIEVRRLA RIGVGGPAVA DLTHLIAELL ENATVFSPPH
     TAVQVHGERV SNGFTLEIHD RGLGMAPEIL LDANLRLAET PDFELSDTDR LGLFVVSRLA
     QRQNVRVSLQ KSPYGGTTAV VFIPAALLTD APDTHGTGFR LDRRAERAIG SGRNSDAAQG
     PQSTAPGGER RVNGRSPALA PVPTGLTAPG VLDGPVELEA PVGPLDFTGD PLDRSPEPEL
     DPALGPVLDG VSDLEDTESE RGGIFRARDL RRDGDREPRR DEPGGRRRAT DRDQHQQARD
     HGDEPTAQVR PVRPAGPVPL PRRTPPTLVT DRGRRVDDPG EDRVDTPARA TGPVPHTVDR
     EPGEAGRSRS RTADAPWTVR AAGHRTTEAS RATETHRTTE APRATEAPRV TESAPPAPDT
     VGGLPRRVRQ ASLARQLREE AVERTPRRAP ADTFDDDERD ADEVRDRMAS LQRGWQRGRR
     QNAAESTENT ENTESTDDTG NTEDTGGPGG TAPGTTPGGD GR
//
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