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Database: UniProt
Entry: A3TK11_9MICO
LinkDB: A3TK11_9MICO
Original site: A3TK11_9MICO 
ID   A3TK11_9MICO            Unreviewed;       357 AA.
AC   A3TK11;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=JNB_01070 {ECO:0000313|EMBL:EAP98716.1};
OS   Janibacter sp. HTCC2649.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP98716.1, ECO:0000313|Proteomes:UP000005063};
RN   [1] {ECO:0000313|EMBL:EAP98716.1, ECO:0000313|Proteomes:UP000005063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP98716.1,
RC   ECO:0000313|Proteomes:UP000005063};
RX   PubMed=21075932; DOI=10.1128/JB.01298-10;
RA   Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J.,
RA   Vergin K.L., Giovannoni S.J.;
RT   "Genome sequence of the Marine Janibacter Sp. Strain HTCC2649.";
RL   J. Bacteriol. 193:584-585(2011).
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:EAP98716.1}.
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DR   EMBL; AAMN01000002; EAP98716.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3TK11; -.
DR   STRING; 313589.JNB_01070; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_3_11; -.
DR   Proteomes; UP000005063; 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; 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: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; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005063};
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        50..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          79..132
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          140..356
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          334..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   357 AA;  37621 MW;  C383905A69A1AD86 CRC64;
     MLIAQTLVLV ACAVTSWLVA SVVGPSIFHD HLQQAGVGHS PSEAAHVEEA FGSALLISLG
     VALTASVLLA LGVTAFFTRR VQRSTAAVAH SASRIAGGNY QSQVPSPGLG AEFDQLATTI
     NDLAQRLGDV ETTRRRLLAD LAHEMRTPLG SIEAHLEAIE DGIRSLDHAT LEVLHGNTTR
     LQRLAEDITA VARAEEGGLD LRPVPTDTTT LVESATAAAH NAYDVKQIAL DVDTRPTGTV
     LVDPDRMAQV LANLLDNALQ HTPPGGRVRV AVRKPDPDWV EITVTDNGEG IDAHHLVHVF
     ERFYRADPAR SRVRGGSGIG LTISKALVEA HGGGLSASSP GPGGGAEFTL RLPLDRA
//
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