ID A0A2P4UR27_9ACTN Unreviewed; 502 AA.
AC A0A2P4UR27;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cusS_3 {ECO:0000313|EMBL:POM27502.1};
GN ORFNames=BTM25_19170 {ECO:0000313|EMBL:POM27502.1};
OS Actinomadura rubteroloni.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1926885 {ECO:0000313|EMBL:POM27502.1, ECO:0000313|Proteomes:UP000242367};
RN [1] {ECO:0000313|EMBL:POM27502.1, ECO:0000313|Proteomes:UP000242367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2 {ECO:0000313|EMBL:POM27502.1,
RC ECO:0000313|Proteomes:UP000242367};
RX PubMed=28463423; DOI=10.1002/chem.201701005;
RA Guo H., Benndorf R., Leichnitz D., Klassen J.L., Vollmers J., Gorls H.,
RA Steinacker M., Weigel C., Dahse H.M., Kaster A.K., de Beer Z.W.,
RA Poulsen M., Beemelmanns C.;
RT "Isolation, Biosynthesis and Chemical Modifications of Rubterolones A-F:
RT Rare Tropolone Alkaloids from Actinomadura sp. 5-2.";
RL Chemistry 23:9338-9345(2017).
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:POM27502.1}.
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DR EMBL; MTBP01000001; POM27502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P4UR27; -.
DR Proteomes; UP000242367; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 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; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 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:POM27502.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000242367};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:POM27502.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 61..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..283
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 291..501
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 53720 MW; 90EE070EA2BBDC99 CRC64;
MRRPGGGGAA RPAAAGNGPP QDASDNSDNS DNQEPAGRAR RGRIMRLVPR WRQPPRIRLR
VTLSAILITA VLTLAVYVLL LLLIRRQEVS SVDHELGQES SRLVAIVQGG LPDDGRILTG
DSQELLQVIG PGGKIAAANE EMIGEPPVAF PPPGRGEERR LGTACGISAP GGRCFRVFVR
RAVTAHGEFF AYALLPAPGL VPRPGEAAVL AIGIPLVTGL IGAGTWRAAG RTLRPVDEIR
ADLDEITASD LQRRVPVPPR DDEISRLAAS VNATLDRLEA AVARQRGFVS DVSHELRSPL
AGLRTELEVA LADPDASDVR ETLDATLRSA DRLQAVVEDL LALARLDSSD RGPDEPVELH
GLADQEVLRR PRRSRIIVPD GDPVTVRGSP RDLARLFTNL IDNADRHAAS EVIVRIGTLP
GSYAVVEVVD DGTGIAPEDR ERIFERFTRL AEGQHRDAGG TGLGLAIARD IAAAHQGSLV
LQDRADGQEG ARFVLLLPMQ AE
//