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Database: UniProt
Entry: A0A1I4SWZ1_9ACTN
LinkDB: A0A1I4SWZ1_9ACTN
Original site: A0A1I4SWZ1_9ACTN 
ID   A0A1I4SWZ1_9ACTN        Unreviewed;       573 AA.
AC   A0A1I4SWZ1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04487980_100486 {ECO:0000313|EMBL:SFM68974.1};
OS   Streptomyces sp. cf124.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFM68974.1, ECO:0000313|Proteomes:UP000198530};
RN   [1] {ECO:0000313|EMBL:SFM68974.1, ECO:0000313|Proteomes:UP000198530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF124 {ECO:0000313|EMBL:SFM68974.1,
RC   ECO:0000313|Proteomes:UP000198530};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR   EMBL; FOUV01000004; SFM68974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4SWZ1; -.
DR   Proteomes; UP000198530; 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; 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; 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:SFM68974.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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}.
FT   TRANSMEM        232..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          258..311
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          319..539
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          139..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  59735 MW;  179EA2C53D22AD09 CRC64;
     MTRRLLLSYL SLAALVLLGL EIPLGFVYSR AERERIVNSA NDEAESVAAF TALSLAADRP
     DELVERARHC AERIGGRVVI VDADGELLAS SHSLSVEEKQ SLSSLPEISA ALRGRATTDV
     RTTTTGGVHY LSVAAPVGHA TAGTDTDSGT DPDSGTDTGS DPGSGAKTAP VTYTVSGTGT
     GTGTTADPLP ASHTHPASHT HPASGTRPES GAAAQGAVRI TLPTTMVHAR VFAAWLLLAL
     AGLAVLTGVA AVAFAFARWT GRPIRQLEEA THRLAEGGTA TSVVVTSGPP EVRSLAAAFN
     TTAARLEHLL ASQRAFAGEA SHQLKTPLAA LRLRLENLEP DIARRARPSL DAAVTETDRL
     ARMVEGLLAM ARLEESAAIP APVDLGAICA ERHRTWGPLF EREGVSLVLF AGVVGPVTAV
     PGAVEQILDN LLSNALRASP AYSTVTMELR LLVPARRALR DARPSWVDLH VTDEGPGMTP
     EQRARAFDRF WRAPGAPKGG TGLGLSLVQR LAHASGGEVT LREAATGGLD AVVRLPSAEP
     PGPVHGHGHS HGHGHGFGGR PGQRRREAPP LPA
//
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