ID D9X438_STRVT Unreviewed; 737 AA.
AC D9X438;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SSQG_06384 {ECO:0000313|EMBL:EFL35866.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL35866.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) 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};
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DR EMBL; GG657757; EFL35866.1; -; Genomic_DNA.
DR AlphaFoldDB; D9X438; -.
DR STRING; 591159.SSQG_06384; -.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_002554_3_1_11; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; IPR013587; Nitrate/nitrite_sensing.
DR InterPro; IPR010910; Nitrate/nitrite_sensing_bac.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08376; NIT; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50906; NIT; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000004184};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..346
FT /note="NIT"
FT /evidence="ECO:0000259|PROSITE:PS50906"
FT DOMAIN 377..448
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 565..673
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 79286 MW; 154EDFD1CFEFE0E2 CRC64;
MTPDPWPRGA AAQERLHPLH PRVGRAHRTR PRPRHWPDAR TARHLARARN WRVRSKLTAV
VLIPGLLAGF LATVSLSRTI GDARDYGRFA ALARLQRPAL GLVHALQDER DDTAAFVAER
REGSRGSLDE RRAAADTAAV AYRRAAGALD AAGDPRLEVA SRRAAEELRT LGGLRRAVDE
AGLTQGAIVA GYTVMVSRLM DLGPVLAEHN GDGTSAQRVR VLNTLSVAVE NTSRVRAELN
AALTTGTFLV GQFPEFAGAV ARQQESVDDF LATTSLPQRT LYADSVKGTS VSAAQAIQER
AAEQAQAGRI GIEPARWKQV SGRKIALMRT VESRVLDDLI SVSDAAHAAR LWAGWWGAAG
MLAVFLATGG MVTAAVRSMT RPLRTLRASA LDVAHHRLPA ALERLRQADV DDLGDIRAEP
TGVVCEDEIG EVARAFDAVH DAAVRLATDQ AALRSHINGM FVHLSRRNQR LVGKLLTEIG
DLEQDERDPE RLARLFQLDH LATQMLRTDE SLLVLAGSDT GRGWDRPMPL AEVLLAASAE
VEHYARVVCR PSVEADVVGD AVTDLVHLLA ELMENATQFS GPRSTVMVTY GVARDRAAGL
VITIVDEGSG MTPADLALAN HRLSSVRAFD PEAGQTMGLF VVSRLASRHG ISVALVPSPR
RGTTALVRLP RHLLARLEDP SAAEAAHPHA LAAQVPPAAP AFGSAQDWLV HRRFSDGLHA
DAGHAPPSVP FTTEGQP
//
