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Database: UniProt
Entry: A0A0B5F6Z2_STRA4
LinkDB: A0A0B5F6Z2_STRA4
Original site: A0A0B5F6Z2_STRA4 
ID   A0A0B5F6Z2_STRA4        Unreviewed;       517 AA.
AC   A0A0B5F6Z2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SLNWT_6275 {ECO:0000313|EMBL:AJE86651.1};
OS   Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS   NBRC 107858).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE86651.1, ECO:0000313|Proteomes:UP000031523};
RN   [1] {ECO:0000313|EMBL:AJE86651.1, ECO:0000313|Proteomes:UP000031523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC   {ECO:0000313|Proteomes:UP000031523};
RA   Lu C.;
RT   "Enhanced salinomycin production by adjusting the supply of polyketide
RT   extender units in Streptomyce albus DSM 41398.";
RL   Submitted (JAN-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};
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DR   EMBL; CP010519; AJE86651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B5F6Z2; -.
DR   KEGG; sals:SLNWT_6275; -.
DR   Proteomes; UP000031523; Chromosome.
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   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AJE86651.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031523};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        17..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          261..375
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          440..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  55606 MW;  AFB9CE15350D11F8 CRC64;
     MSVEPPPTGR EVPYARVLLL PAVLMAAVAG GAAALVDEGA RPAVAVCGAV CLLLVLAVAA
     QAVRGFRTAR RLRARHAHQI AFLKRRTDAH EEQSVRLGRD LLPEALLRLG RGESPAEVVQ
     ALVDADPVHR DLPMAGRALL RDVLEIVDNE RAMRESAQLA FVNIARRVQA IVHRQAAELR
     EMEEDHGRNP EVFDDLLRID HGTALIGRLA DSVTVLGGAR PGRQWPGPVP LFSVLRGAMS
     RILDYQRVDL HSLVDVAVLG TSVEPLIHAC AELLDNATRY SPPQTRVHVT AVEVQTGIAI
     EIEDGGVSLS EEARARAERM LAQAQVGIDL NDLGETPRLG MAVVGRLAQM YGMQVSLRQS
     AYGGVRAVLV VPREMLTTAP APALAHGIGA AAVPRVNEEG RLIEEPARPA KRHRQPTGPV
     ASPPLVPAVV AESFDPPPIE EWTPNGLPQR RSRVRSSYTR RLAERAQAAP AREVPSGGGE
     PEPGLWIEAF MTGASGSDET SADGRRHPAS EEEGNHQ
//
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