ID A0A0X3UTY8_9ACTN Unreviewed; 535 AA.
AC A0A0X3UTY8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ADL22_30205 {ECO:0000313|EMBL:KUL34336.1};
OS Streptomyces sp. NRRL F-4489.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL34336.1, ECO:0000313|Proteomes:UP000053256};
RN [1] {ECO:0000313|EMBL:KUL34336.1, ECO:0000313|Proteomes:UP000053256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL34336.1,
RC ECO:0000313|Proteomes:UP000053256};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KUL34336.1}.
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DR EMBL; LLZI01000276; KUL34336.1; -; Genomic_DNA.
DR RefSeq; WP_066987033.1; NZ_LLZI01000276.1.
DR AlphaFoldDB; A0A0X3UTY8; -.
DR STRING; 1609095.ADL22_30205; -.
DR Proteomes; UP000053256; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KUL34336.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053256};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 204..256
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 271..483
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 483..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 237..264
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 484..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 57468 MW; F3DDC070E0E493D2 CRC64;
MRRLRRLVPG VSAVRGLRAR LVVAFLLVAA VSALTTAGLT YREARNAILQ RSQDTAVNDL
RAQVDSLAPE LTVPPSRADL DFFRVQLERS GKSRDWDISV HYNGMPDSDE GGLRREVVVP
AGFKTSVEKR RVPAFQRIDR DGDPWLLIGM PVRQSDGGAS PLTVYAQLPL RAEEANVEAL
VRAARGGALP AFALAVILPL IAARGVLRPV RGLRQAAGRI AEGKLDTRLV VKGTDELADL
SRTFNEMAAK LEESMAELRR MEANSRRFAA DVSHELRTPL AAMTAVTDVL DEDADSLDPD
TASAVRLISQ ETGKLARMVE DLMEVSRFDA GAAALHLYEV DVAETIRKTL QARAWQQRVE
AELPDGVRAR LDPRRLDVVV ANLVGNALHH GGEPVRVVLH APEPGDPTLL IEIRDSGPGI
DPEVLPHVFD RFYKADSARA RSEGSGLGLA IAQENVRLHG GTLRAANAPE GGAVFTVELP
LRQEEAPAGE EPGERDGDGN GDGGAPRSGA RDGRSPKTGA SDAGAQDGGK DGDAR
//
