ID A0A177HHC0_9ACTN Unreviewed; 1227 AA.
AC A0A177HHC0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=STSP_63390 {ECO:0000313|EMBL:OAH10341.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH10341.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH10341.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-2015) 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};
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:OAH10341.1}.
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DR EMBL; LOHS01000150; OAH10341.1; -; Genomic_DNA.
DR RefSeq; WP_067284343.1; NZ_LOHS01000150.1.
DR AlphaFoldDB; A0A177HHC0; -.
DR STRING; 1716141.STSP_63390; -.
DR PATRIC; fig|1716141.3.peg.6667; -.
DR OrthoDB; 4652229at2; -.
DR Proteomes; UP000077381; 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 CDD; cd06225; HAMP; 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; 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; PF00672; HAMP; 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:UP000077381};
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 392..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..384
FT /note="NIT"
FT /evidence="ECO:0000259|PROSITE:PS50906"
FT DOMAIN 415..485
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 602..708
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 128388 MW; 554418FCE49EB771 CRC64;
MQGRFKRDSS AAAENEPHGG TDRGSSPQHA QSPGPGPSGD GGGARTGAPG AGLPAAQPKP
KTPTGPGSRL ALRNWRISTR LVALMTLPVV AATSLGALRI SESMDDIQQL DNMKLLTDMT
KQATDLAAAL QDERDQSAGP LSHGADDTDF AIKGPRDTTD RLVKSFREGT REIQDADDGQ
SLDGVRDHVV QIQRQLATLK SIRKDAYTDP DNSSQTVDAY SRLIEELLSL STDMAQATSN
PEMIQRTRAL AAFSTAKEYA SVQRAIIAAA LPANDSQVGK LSETDRRYAA AAADNEDSEL
TAFTNIYNSY GGNAAELTKP IDKGNATITA ADDYAEGALR EGGLRLQEKR SYKDWVDADS
AKIDQMGKIE LTLLDEMEQK ARELRSESER EAYISGALIL LVLGISLVGA FVVARSMIRS
LRRLQDTATR VAQDRLPELV KQLSESDPQD VDTSVESVGV HSRDEIGKVA SAFDDVHREA
VRLAAEQALL RGNVNAMFTN LSRRSQGLIQ RQLSLISELE SREADPDQLS SLFKLDHLAT
RMRRNGENLL VLAGEEPGRR WTRPVPLVDV LRAAASEVEQ YERIELAAVP ATEVAGRVVN
DLVHLLAELL ENATSFSSPQ TKVKVTGHAL PDGRVLIEIH DTGIGLSPED LAAINERLAS
PPTVDVSVSR RMGLFVVGRL SQRHGIRIQL RPSDSGGTTA LVMLPVDVAQ GGKKAPGKPG
PGGSGGPAAA QAAAGAAAAR RGVGAGASAG ASAGRLGAGP GPRGQVGAGA GPRAALPSRD
PEPGRPGPQS GPGGLFGGPQ DGPSSPQQGQ GRHASAGAGA GAGAGALRQG PPHSGPRAAQ
GRTGDSADEG RMPQLPPHGG PRAELPGGNP KPRVPSVPSW SNETGRPPVS RASLDTPRGH
EEPESTAPIP RVDGRQGPGP GARYPSPVSD DRQGPGSTAE FARPDFDAPR PGSQPAQGPG
AHPGANAPGN TGQFVRPDVF GGPNPSGATG QFPAPGYQSP QQTPQDSAST GQFERPAAGG
GQPRGDRDGF DTRGGHGAPR PPAHRADRIP QQPAGPAREP EALPPASGPG DGRTPLFDTL
ETNWFRQQGG GERPTDPQQQ PSQPQAPAAP VAPAHTPAAA SQPGPSGPTA AAWRSSPNDE
LVRQAERVRK PSAGGVTTSG LPRRVPRANL VPGTAQQQQH QTGPQVSRAP DDVRGRLTNL
RRGIQQGRQA GTGQTGSFPR PTHQQER
//
