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Database: UniProt
Entry: A0R408_MYCS2
LinkDB: A0R408_MYCS2
Original site: A0R408_MYCS2 
ID   A0R408_MYCS2            Unreviewed;       446 AA.
AC   A0R408;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=MSMEG_5663 {ECO:0000313|EMBL:ABK75033.1};
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK75033.1, ECO:0000313|Proteomes:UP000000757};
RN   [1] {ECO:0000313|EMBL:ABK75033.1, ECO:0000313|Proteomes:UP000000757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) 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; CP000480; ABK75033.1; -; Genomic_DNA.
DR   RefSeq; WP_011730694.1; NZ_SIJM01000034.1.
DR   RefSeq; YP_889896.1; NC_008596.1.
DR   AlphaFoldDB; A0R408; -.
DR   STRING; 246196.MSMEG_5663; -.
DR   PaxDb; 246196-MSMEI_5514; -.
DR   GeneID; 66736959; -.
DR   KEGG; msm:MSMEG_5663; -.
DR   PATRIC; fig|246196.19.peg.5519; -.
DR   eggNOG; COG2205; Bacteria.
DR   OrthoDB; 5241347at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   GO; GO:0005886; C:plasma 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABK75033.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABK75033.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          170..222
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          237..446
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   446 AA;  47819 MW;  30EE7E48CCA7108C CRC64;
     MSMLTRIFRR TPSLRTRVAF ATAIGAAIVV VIVGTIVWIG ITNDRKERLD RRLDEAAGFA
     IPFLPRGLDQ IPRSPNDQDA VITVRQTGAV TSNSTVVLPE LPAGYADTYI DGVRWRVRTV
     EIPAPGPMWV AVGATYDATI ADTNNLHRRV LVICVFAVGA ATVLGWVLAA FAVRPLKRLA
     EQTREIEAGD EAPDVEVRGA TEAVEIAEAV NGMLKRIWKE QDRTKSALAS ARDFASVSAH
     ELRTPLTAMR TNLEVLSTLD LPDEQRKEVV NDVIRTQSRI EATLGALERL AQGELSTTDD
     HVTVDITELL DRAAHDAMRI YPDLEVSLAP SPTVIIVGLP TGLRLSVDNA IANAVKHGGA
     TRVQLSAVSS REGVEIAIDD NGVGVPEGER ALVFDRFARG STASRSGSGL GLALVAQQAE
     LHGGTATLAE SPLGGARLLL RLPGPR
//
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