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Database: UniProt
Entry: L1KRR2_9ACTN
LinkDB: L1KRR2_9ACTN
Original site: L1KRR2_9ACTN 
ID   L1KRR2_9ACTN            Unreviewed;       467 AA.
AC   L1KRR2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-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=STRIP9103_02499 {ECO:0000313|EMBL:EKX63486.1};
OS   Streptomyces ipomoeae 91-03.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX63486.1, ECO:0000313|Proteomes:UP000010411};
RN   [1] {ECO:0000313|EMBL:EKX63486.1, ECO:0000313|Proteomes:UP000010411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91-03 {ECO:0000313|EMBL:EKX63486.1,
RC   ECO:0000313|Proteomes:UP000010411};
RA   Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL   Submitted (NOV-2012) 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:EKX63486.1}.
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DR   EMBL; AEJC01000429; EKX63486.1; -; Genomic_DNA.
DR   RefSeq; WP_009326288.1; NZ_AEJC01000429.1.
DR   AlphaFoldDB; L1KRR2; -.
DR   PATRIC; fig|698759.3.peg.5849; -.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000010411; 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; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:EKX63486.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010411};
KW   Transferase {ECO:0000313|EMBL:EKX63486.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        18..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          253..467
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   467 AA;  48658 MW;  8678D62703771967 CRC64;
     MDLQHPGGRR RRSTGRRLAA AGAAAAGLAV LTAALVPLRD SLSLASVVLI YLTAVVIVAA
     TGGLPMALAA AVASDVLVNF FFVPPFHTLT VEDRDLFITL AVYVAVATTV SVAVDLAARQ
     RAAAARSGVE AALLARITQA PLEERPLSAV LEHVRDTFGM TGAALLERDA DGERPVAVVG
     EPPSADPTLS APAGEDLRLV ADGPAVFAAD ERFLTLLATA AARALQAERL AAQAARAREL
     TEIDKLRAAL LAAVGHDLRT PLAGIKACVS SLREPDLELT DAQQAELLAT VDASADKMSD
     LVENLLALSR LQAGALSVHP RPTALDEITA AALLHTPPAP GRAVDVDVPD DLPPAWADPG
     LLERVIANLV ANALDAGPPD QPVHVHARQE GNMIRLRITD HGPGVPADQR ERIFAPFQRL
     DDHTTRHGLG LGLAIARGFT EAMNGTLTPT DTPGGGLTMT LTFPTAP
//
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