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Database: UniProt
Entry: I0HBY2_ACTM4
LinkDB: I0HBY2_ACTM4
Original site: I0HBY2_ACTM4 
ID   I0HBY2_ACTM4            Unreviewed;       468 AA.
AC   I0HBY2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=AMIS_52990 {ECO:0000313|EMBL:BAL90519.1};
OS   Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS   JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL90519.1, ECO:0000313|Proteomes:UP000007882};
RN   [1] {ECO:0000313|EMBL:BAL90519.1, ECO:0000313|Proteomes:UP000007882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC   NCIMB 12654 / NRRL B-3342 / UNCC 431
RC   {ECO:0000313|Proteomes:UP000007882};
RA   Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA   Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT   "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT   102363).";
RL   Submitted (FEB-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};
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DR   EMBL; AP012319; BAL90519.1; -; Genomic_DNA.
DR   RefSeq; WP_014445407.1; NC_017093.1.
DR   AlphaFoldDB; I0HBY2; -.
DR   STRING; 512565.AMIS_52990; -.
DR   KEGG; ams:AMIS_52990; -.
DR   PATRIC; fig|512565.3.peg.5293; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_89_6_11; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000007882; Chromosome.
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, ECO:0000313|EMBL:BAL90519.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007882};
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        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          183..241
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          249..467
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   468 AA;  49291 MW;  D2DA9972FDDBD5E7 CRC64;
     MTLWWRERTL HARLALLVAG AVAAAVLVVS AGAWFTVREI QQDKVAAELA SDASTIAANP
     AYWLAMEGKR EASGYRHGKE IGPCWQIIDA SGTVVGGTAT PLPVTDAAVA VAAGSSEPVR
     EEVTLGPGEY LMFTKPLPGG GAVQVALDRR PDDRVLMTFA LLLAVGCAAG IGGAALLGRT
     VSRAGLAPVD RLTGAVEDVA VTMDLSRWAQ ARPIEVAGND EIARLGRSVN TMLSTLDASR
     RAQRALVEDA GHELRTPLTS IRTNVELLLT VERNPELAHR LTTEDRTSLL EDLDAQVREL
     ATLTTELVEL SREEASREAV EPLDLAEVVT AAVSRVQLRA PALTFDTALT PATVLGRPGE
     LERMVVNVLD NAAKWSPPAG KVQVRLIPDG PGACLLTVTD TGPGIADEDR PHVFDRFYRS
     AAARAMPGSG LGLAIVAQTA TNHGGTVQAL PNSPTGTILT IRLPGTPA
//
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