ID A0A2U2Z3W8_9ACTN Unreviewed; 505 AA.
AC A0A2U2Z3W8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DIZ27_30440 {ECO:0000313|EMBL:PWI06919.1};
OS Streptomyces sp. NWU339.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2185284 {ECO:0000313|EMBL:PWI06919.1, ECO:0000313|Proteomes:UP000245372};
RN [1] {ECO:0000313|EMBL:PWI06919.1, ECO:0000313|Proteomes:UP000245372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWU339 {ECO:0000313|EMBL:PWI06919.1,
RC ECO:0000313|Proteomes:UP000245372};
RA Adegboye M.F., Lobb B., Babalola O., Doxey A.C., Ma K.;
RT "Draft genomes of two novel cellulolytic Streptomyces strains isolated from
RT South African rhizosphere soils.";
RL Submitted (MAY-2018) 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:PWI06919.1}.
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DR EMBL; QFRK01000034; PWI06919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2Z3W8; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000245372; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF48; TWO-COMPONENT SENSOR HISTIDINE KINASE-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PWI06919.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245372};
KW Transferase {ECO:0000313|EMBL:PWI06919.1}.
FT DOMAIN 44..124
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 296..475
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 480..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 55304 MW; C75DE18EFDB748FD CRC64;
MSGRPMPCSP EEIGSLFLFE KLSGEQLGRL CREGRIERFD PGPVYTEGEP AACFYVMLEG
TVVLSRRVGG DDVEVIRSSQ RGVYSGAMQA YLGDRLRQVY NNSMRVTEPT RFFVLPAETF
ADIMREWFPM AVHLLEGLFF GSKSTQAAVG QRERLLALGS LSAGLTHELN NPAAAAVRAT
ATLRERVARM RHKLALIAGS SFSRDQLANL IDIQQRTAER VAKAPVLTPL EVADREDALT
DWLEDHGIEQ GWQIAPTFVQ AGLDVDWLEQ VAASVGQEIL PGAVGWLNYT VETELLMDEI
ADSTTRVSRL VDAAKQYSQL DRAPYQVADV HELLDSTLLM LSGKIGPRIR IAKEYDRTLP
RIPAYPAELN QVWTNLIDNA LCAMDGAGGD GTLTVRTALH DNQLLVEFRD TGPGVPPEIR
DRIFDPFFTT KPVGRGTGLG LDISRRIVVN KHHGSIGVES VPGDTRFRVL LPLAAVEPDG
TALSSAASDG PPLTSEDRTT SQEPA
//
