ID A0A1Q4VVJ0_9ACTN Unreviewed; 503 AA.
AC A0A1Q4VVJ0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMK13_30840 {ECO:0000313|EMBL:OKI01818.1};
OS Streptomyces sp. CB02056.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703924 {ECO:0000313|EMBL:OKI01818.1, ECO:0000313|Proteomes:UP000186379};
RN [1] {ECO:0000313|EMBL:OKI01818.1, ECO:0000313|Proteomes:UP000186379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02056 {ECO:0000313|EMBL:OKI01818.1,
RC ECO:0000313|Proteomes:UP000186379};
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 -!- 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:OKI01818.1}.
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; LIPD01000013; OKI01818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4VVJ0; -.
DR OrthoDB; 3206505at2; -.
DR Proteomes; UP000186379; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OKI01818.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000186379};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 214..272
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 280..483
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 106..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 50510 MW; 49FD9CE6AA5EDC79 CRC64;
MRWALIKAAV AGTTMVALAF LIPLGLMVQQ TARDRAFTAA ERQAAALGPA LAITTDEDAV
NRALASTDAG GQGRMAVHLP AAGQPAGAGG AEAAAVGTGG GAPGTVAAGT GGGGPAAAAA
GTGEPEGPML GEGRAAAADV ATAGGKGRSF TVKVAGGYAL LQPVAVDTGR TAVVEVFVAE
SDLTRGVATA WQVLSAVALG LVAISVLVAD RMGSRIVASA RKLAAAARSL GAGNLAVRVP
VEGRLVAGSP EELREAGQAF NTMADRVVQL LAAERELAAD LSHRLRTPLT VLRLNAASLG
EGDAADATRH AVAQLEREVD QIIRSARRAP EDAPVVAVGC DAAEVIRERV AFWSALAEDE
GRRWQLAGAE RAAPVPVQRG DLAAAVDALL GNVFRHTAVG TAFSVDVLAT DCSVIVLVGD
AGPGYSDPAA ALKRGEGHGG EGSTGLGLDI VRKLAESTGG DLALGRSAVL GGAETRLRLR
TGPQEAAPAR GGRRRSRGAL FQK
//
