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Database: UniProt
Entry: R4T9W1_9PSEU
LinkDB: R4T9W1_9PSEU
Original site: R4T9W1_9PSEU 
ID   R4T9W1_9PSEU            Unreviewed;       534 AA.
AC   R4T9W1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AORI_5093 {ECO:0000313|EMBL:AGM07677.1};
OS   Amycolatopsis keratiniphila.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX   NCBI_TaxID=129921 {ECO:0000313|EMBL:AGM07677.1, ECO:0000313|Proteomes:UP000013968};
RN   [1] {ECO:0000313|EMBL:AGM07677.1, ECO:0000313|Proteomes:UP000013968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCCB10007 {ECO:0000313|EMBL:AGM07677.1,
RC   ECO:0000313|Proteomes:UP000013968};
RX   PubMed=23627759; DOI=10.1186/1471-2164-14-289;
RA   Tang B., Wang Q., Yang M., Xie F., Zhu Y., Zhuo Y., Wang S., Gao H.,
RA   Ding X., Zhang L., Zhao G., Zheng H.;
RT   "ContigScape: a Cytoscape plugin facilitating microbial genome gap
RT   closing.";
RL   BMC Genomics 14:289-289(2013).
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};
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DR   EMBL; CP003410; AGM07677.1; -; Genomic_DNA.
DR   RefSeq; WP_016335419.1; NC_021252.1.
DR   AlphaFoldDB; R4T9W1; -.
DR   KEGG; aoi:AORI_5093; -.
DR   PATRIC; fig|1156913.3.peg.5183; -.
DR   HOGENOM; CLU_020211_11_1_11; -.
DR   Proteomes; UP000013968; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00130; PAS; 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   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGM07677.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        176..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          317..531
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   534 AA;  56425 MW;  EA505D366A2B0B74 CRC64;
     MPSTTRIRTR RGSLARQLLI LQLVVLFVLV AAGVTFAYLD SVRATEDRAR DKVTAVAEAV
     ADAPGVLAAL STSEPTRTLQ PFAQSVRADT DVDFVTIMDK NGIRYTHPNP ALIGQRFIGN
     IGEAQRGGKV VETYAGSLGP SERVVVPVRG AAGQVVALVS VGITVEAIDA ELRERLWPLL
     GVAAAVLVVG GIGSYLVSAR LRRQTRGIAP EELSNLFEYH EAVLHSVREG LLLVGGDGRV
     VLCNDGARAL LGVDEDVVGR ELSELDIPED LVEAFASGEE RTDELHLTDA RVLVVSTSPV
     RSRGKAMGTV VILRDHTELQ ALTGELTTVR GLAEALRSQA HEAANRLHTV VSLVEIGRPE
     QAVEFATEEL ALAQELTDRV VGAVAEPVLA ALLLGKAAEA SERGVEFTIT PDTVMEDSDT
     GVPPRDLVTI LGNLIDNGID AAAGNAGHGG RPGVEVTVRS GAEGLLLRVA DTGPGVDDVE
     DVFRRGWSTK PEDGHGLGLA LVGQAVRRHS GTIDVGRDEG AVFTVCLPPK EPAR
//
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