ID A0A1Q5JTV8_9ACTN Unreviewed; 912 AA.
AC A0A1Q5JTV8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:OKJ72749.1};
GN ORFNames=AMK31_33780 {ECO:0000313|EMBL:OKJ72749.1};
OS Streptomyces sp. TSRI0107.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ72749.1, ECO:0000313|Proteomes:UP000185813};
RN [1] {ECO:0000313|EMBL:OKJ72749.1, ECO:0000313|Proteomes:UP000185813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ72749.1,
RC ECO:0000313|Proteomes:UP000185813};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ72749.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LIVZ01000015; OKJ72749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5JTV8; -.
DR STRING; 1703942.AMK31_33780; -.
DR Proteomes; UP000185813; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd16936; HATPase_RsbW-like; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR PANTHER; PTHR43156:SF2; MULTIDOMAIN REGULATORY PROTEIN RV1364C; 1.
DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OKJ72749.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000185813};
KW Transferase {ECO:0000313|EMBL:OKJ72749.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..281
FT /note="PAS"
FT /evidence="ECO:0000259|SMART:SM00091"
FT DOMAIN 346..512
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT DOMAIN 530..756
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|SMART:SM00331"
SQ SEQUENCE 912 AA; 98151 MW; A0354BB29015D0DA CRC64;
MLNLRSAAGQ VFLLQIVIVV LLVAAAVVGM VLQAASDALQ QGRRESVVAA QTFANAPGTA
AALQSPDPSA VLQPRAEEAR KRAGMDFIVA MNTEGIRYTY PYPQEIGKKF VGTIEPALQG
RTVVEQAGGP PLPVGKGTNV QAVVPVTDSR GEVVGLVSAG LTVKNVAQLW LPQLPIILGS
GAAALVLAIA GTTLVIRRLR RQTRGLAPVE LAQLYEHHDA VLHAVREGVL IIGPDGRLLL
ANDEAMRLLG LPEQVQGRPV RELGLPEPML RLLSSPDAVT DEVHSVGNRM LAVNKRPTYP
HDDRAGSVVT LRDTTELAAV SGRAEVARER LKLLYEAGMG IGTTLDVGRT AQELADVAAR
QFADLVTVDL LDAVLRGWEP TAEGWRHLRR AAIGGDHQRV PVYRLGEVIT FSVHTPQMRT
LQEGRGLLET DLSQARGWRE QDPERARKAL ECGLRSLVTV PLRARHVALG VANFYRTADS
PAFEPEDLDI AEELAVRAAV ALDNARRFTR EHAMAVTLQR SLLPRGQPDQ DALEVSWRYL
PAEAGVGGDW FDVIPLPGAR VALVMGDVVG HGLHAAATMG RLRTAVHNFS TLDLPVDEVL
GNLDDLVVRM DNEEGADDAA NGHEGQGVTG ATCLYAVYDP VAGSCTMARA GHPEPMVLLP
DGTVTCPGVP ASAPLGLGGY PFETAEFTVP EGSQLVLYTD GLVEDRAQDI DVGMERLRRA
LDGFGDRSPE ETCQAVMDAL QPSPSFDDIA LLTARTRIYP PSRVAEWDVP PDPALVPSVR
ARCRETLAQW GLEETGYATE LIVSELVTNA IRYGSPPIGV RLLHGRCLTC EVSDGSGTSP
RLRRAATTDE GGRGLFLVAQ FAQRWGTRHT PRGKVIWAEQ FLQDGASGAS HPAPVSFLLD
QFDLDQFDLD QD
//
