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Database: UniProt
Entry: A0A238Y1G6_9PSEU
LinkDB: A0A238Y1G6_9PSEU
Original site: A0A238Y1G6_9PSEU 
ID   A0A238Y1G6_9PSEU        Unreviewed;       566 AA.
AC   A0A238Y1G6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN06265360_11326 {ECO:0000313|EMBL:SNR64621.1};
OS   Haloechinothrix alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Haloechinothrix.
OX   NCBI_TaxID=664784 {ECO:0000313|EMBL:SNR64621.1, ECO:0000313|Proteomes:UP000198348};
RN   [1] {ECO:0000313|EMBL:SNR64621.1, ECO:0000313|Proteomes:UP000198348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45207 {ECO:0000313|EMBL:SNR64621.1,
RC   ECO:0000313|Proteomes:UP000198348};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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};
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DR   EMBL; FZNW01000013; SNR64621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238Y1G6; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000198348; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR   PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 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   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SNR64621.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198348};
KW   Transferase {ECO:0000313|EMBL:SNR64621.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        30..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          297..496
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          430..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          271..298
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        496..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  59611 MW;  516829CFA81243A0 CRC64;
     MTSVDVGIGH TNPLPYRLAV PYRWRAGGEL VAVGSLTVTT YAIAVLPGIV ALHPQGTYLV
     LTLAAAGGAA AAAVLAHLIS QISDSAQEKA RLSPLGAGLA MYGIVVVPFN AAQFSSVETI
     AGLDAGRVVA SVTALTLVAV SLRGWESRWS RWWVSLAGWA AVSIGTAVVV ERVPPLASLV
     AGFSWLEAVV LAVSLLLAVA LAGHGLYVCN PLRWRAGLGI ALIGSAHLLH VPADVRLDHA
     AYAAPALRLL GVAVVVLALA LRAREVVLEL RQRRELEARQ AEESVHALRE NQERAATRDH
     ELRNLVAGLS GASEALDSPE QQDAAAIREL GTAMRAELGR LRSMIDGDHG CDEDRHVDVA
     AELTRLVLLH RADGAEIRLD AQPELAAAIP RSALAQVITN LLTNCARHAP GAPVQVTARR
     SGNWVRIAVH DDGPGVPEEA SRATFPRGAR DPRSGGLGIG LHESAALLHR HGGSLALGPS
     FALSGALATL HVPAPSGARH DREAPEPHRP AGRRPRTRRD LTGHGSARGR AGRAQLHRLR
     TGDGSRDSGG TAGRHRASRS RSRRRA
//
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