ID F3ZM13_9ACTN Unreviewed; 1439 AA.
AC F3ZM13;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=STTU_1721 {ECO:0000313|EMBL:EGJ74510.1};
OS Streptomyces sp. Tu6071.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ74510.1};
RN [1] {ECO:0000313|EMBL:EGJ74510.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ74510.1};
RA Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA Gunther S.;
RT "Genome sequence of Streptomyces sp. Tu6071.";
RL Submitted (APR-2011) 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; CM001165; EGJ74510.1; -; Genomic_DNA.
DR RefSeq; WP_007821710.1; NZ_CM001165.1.
DR HOGENOM; CLU_002554_0_1_11; -.
DR Proteomes; UP000003955; Chromosome.
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, ECO:0000313|EMBL:EGJ74510.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 401..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..393
FT /note="NIT"
FT /evidence="ECO:0000259|PROSITE:PS50906"
FT DOMAIN 424..494
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 611..717
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..905
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1439 AA; 152044 MW; 595357DD02C1BDDD CRC64;
MQGRFKRDGS APAEPEPNGA TDRGAAAPHA PQQGLSTAGH EEQGPEGEAP RDKGDKPGKA
DKAEKKAKTK TGPSGPGSRI ALRNWRISTR LVSLLVLPVA AATTLGGIRI SDSLDDIQQL
DNMKLLTDMT KQATELAAAL QDERDQSAGP LSHKVKATDY SVASWRQKTD RQVATFLQNT
KDITGNNELN GVRSNLDAIT KRVAQLKAIR RDAYADDASI TQTVDAYSQL IDQLLSLSQE
MAQATSNPEM VQRTRALAAF SSAKEYASIQ RAVLAAALPP NKSQFGKLSE TDRRYALNAL
SNEDDEINQF KEIYGAYAGD PEDLLKPIDP DEQPTIKGAR DYAQGSLSTQ GGMELRAKRS
YKDWTDSASE EINQMKTIEL TLLGQMEQKA RELRQSAERD AIINGALIIL VLGVSLVGAF
VVSRSMIRSL RRLQDTATKV AQERLPELVG QLSESDPQDV DLSVESVGVH SRDEIGRVAT
AFDDVHREAV RLAAEQAMLR GNVNAMFTNL SRRSQGLIQR QLSLISELES READPDQLSS
LFKLDHLATR MRRNGENLLV LAGEEPGRRW TRPVPLVDVL RAAASEVEQY ERIELSAVPS
TEVAGRVVND LVHLLAELLE NATSFSSPQT KVKVTGHALP DGRVLVEIHD TGIGLSPEDL
AAINERLAAP PTVDVSVSRR MGLFVVGRLS QRHGIRIQLR PSDSGGTTAL VMLPVDVAQG
GRKVPGKPGA PTGQGGPAAA QAAAGAAAAR RAPAGALGGG QGGPGQGGPG QGGPGGKRLG
AAPERGQVGP GGAPRAALPA RGNAPQAPTG RDAFPPVGGG RPPQGPGNLF GDTRQGPPPG
GARPVPPQDN RQDAFGGGRT APIPPQRRAP QGEGQDGRPQ LPPRGGPRAE LPGGPPQPQH
PAPADRQQPA APWEPQAQDA PRGHDEPRGP RQNFAAPRND SGPGSTAQFP AITPDMPAPE
GIGRYEAQGD PASTGAFPAV DPANARGPQG GYGAEDTGSW ARPQEGYAPG GQGQDGGYPP
HQDQRQDQHR EQRHPQQDQG QGAPGRQGQQ GYGYDDARQQ GGWSPQETGQ FPAPGGAPAP
YGQANGYDSG QYPAGSDTGQ FPAASPQQGQ YQGEPYQGAS GTGQFPAPSQ QPGPYQDTSQ
TGQYPAPSQT GQFPAASQTG QFPAPPYPQD GRPGAYAEGP NAQQPRGPRQ AGPQGPQGPQ
APQGQGGFAV SETSSFPVNT GYEPPRAPRP DGPPARELPR RGPAENALPP AGPGDGRTPL
YDTLETSWFR GPQPGGQEQP PEQPEPPHAA EPPRTGASQR SAEETRSPAA APEGGEETAG
QGPGALPAQV GQETWRASPN DELVRQAERV RQPSAGGVTT SGLPRRVPRA NLVPGTAQQQ
PQQQTGPQVS RAPDDVRGRL TNLRRGIQQG RYQAGNSLRP SGENRPNEGY PRPSHQQER
//
