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Database: UniProt
Entry: A0A0X3W3V2_9ACTN
LinkDB: A0A0X3W3V2_9ACTN
Original site: A0A0X3W3V2_9ACTN 
ID   A0A0X3W3V2_9ACTN        Unreviewed;       413 AA.
AC   A0A0X3W3V2;
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=ADL30_26985 {ECO:0000313|EMBL:KUL51518.1};
OS   Streptomyces sp. NRRL S-1521.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL51518.1, ECO:0000313|Proteomes:UP000053420};
RN   [1] {ECO:0000313|EMBL:KUL51518.1, ECO:0000313|Proteomes:UP000053420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL51518.1,
RC   ECO:0000313|Proteomes:UP000053420};
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:KUL51518.1}.
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DR   EMBL; LLZK01000228; KUL51518.1; -; Genomic_DNA.
DR   RefSeq; WP_062780088.1; NZ_LLZK01000228.1.
DR   AlphaFoldDB; A0A0X3W3V2; -.
DR   Proteomes; UP000053420; 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; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 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:KUL51518.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053420};
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        38..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          137..190
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          198..413
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   413 AA;  44754 MW;  C6C290711D91FE0C CRC64;
     MASTPAPPTA PPKPTWDPRK VEPPFPWLRP TIRIRLTLLY GGMFLIAGIL LLSIIYLLAA
     QALNVGSELP FKIVEGRVAS TVCNLPPNPS ADDLNRAMGA CVNEQRQHAL DNLLSRSLLA
     LLGLAVIAFA FGYAMAGRVL SPLGRITRTA RRVAGTDLSR RIELDGPDDE LKELSDTFDE
     MLDRLERAFT AQQRFVGNAS HELRTPLAIN RTLLEVHLSD PGAPPELHQL GKTLLATNER
     SEQLVEGLLL LARSDNQIVE RKPVDLAEVA DRAVDQVLAE ADAKGVEIRG ERGAAVVQGN
     GVLLERIALN LVQNAVRYNV PGNEEGGWVE VTTEAQHGQA VLVVSNTGPV VPAYEIDNLF
     EPFRRLRTER TGSDKGVGLG LSIARSVARA HGGRIIAEPR EGGGLVMRVT LPI
//
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