ID   NARS_MYCTU              Reviewed;         425 AA.
AC   O53857; L0T7P3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 3.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Sensor histidine kinase NarS {ECO:0000303|PubMed:25659431};
DE            EC=2.7.13.3 {ECO:0000269|PubMed:25659431};
GN   Name=narS {ECO:0000303|PubMed:25659431}; OrderedLocusNames=Rv0845;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION, AND GENE NAME.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=12595424; DOI=10.1128/iai.71.3.1134-1140.2003;
RA   Parish T., Smith D.A., Kendall S., Casali N., Bancroft G.J., Stoker N.G.;
RT   "Deletion of two-component regulatory systems increases the virulence of
RT   Mycobacterium tuberculosis.";
RL   Infect. Immun. 71:1134-1140(2003).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT
RP   HIS-241, AND MUTAGENESIS OF HIS-241.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=25659431; DOI=10.1074/jbc.m114.591800;
RA   Malhotra V., Agrawal R., Duncan T.R., Saini D.K., Clark-Curtiss J.E.;
RT   "Mycobacterium tuberculosis response regulators, DevR and NarL, interact in
RT   vivo and co-regulate gene expression during aerobic nitrate metabolism.";
RL   J. Biol. Chem. 290:8294-8309(2015).
CC   -!- FUNCTION: Member of the two-component regulatory system NarS/NarL
CC       involved in gene expression during aerobic nitrate metabolism
CC       (PubMed:25659431). Plays therefore a crucial role in anaerobic survival
CC       of mycobacteria in host. Functions as a sensor protein kinase which is
CC       autophosphorylated at a histidine residue and transfers its phosphate
CC       group to the conserved aspartic acid residue in the regulatory domain
CC       of NarL (PubMed:25659431). In turn, NarL binds to the upstream promoter
CC       regions of target genes to regulate their expression during aerobic
CC       nitrate metabolism (PubMed:25659431). {ECO:0000269|PubMed:25659431}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:25659431};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- PTM: Autophosphorylated on His-241. {ECO:0000269|PubMed:25659431}.
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DR   EMBL; AL123456; CCP43593.1; -; Genomic_DNA.
DR   PIR; E70813; E70813.
DR   RefSeq; NP_215360.1; NC_000962.3.
DR   RefSeq; WP_003898611.1; NC_018143.2.
DR   AlphaFoldDB; O53857; -.
DR   SMR; O53857; -.
DR   STRING; 83332.Rv0845; -.
DR   PaxDb; O53857; -.
DR   DNASU; 885218; -.
DR   GeneID; 885218; -.
DR   KEGG; mtu:Rv0845; -.
DR   TubercuList; Rv0845; -.
DR   eggNOG; COG4585; Bacteria.
DR   InParanoid; O53857; -.
DR   OMA; VAFQDRP; -.
DR   PhylomeDB; O53857; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Kinase; Membrane; Phosphoprotein; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..425
FT                   /note="Sensor histidine kinase NarS"
FT                   /id="PRO_0000401133"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          224..425
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         241
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT                   ECO:0000269|PubMed:25659431"
FT   MUTAGEN         241
FT                   /note="H->Q: Complete loss of autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:25659431"
SQ   SEQUENCE   425 AA;  45784 MW;  D516B55C22FAA619 CRC64;
     MPSYGNLGRL GGRHEYGVLV AMTSSAELDR VRWAHQLRSY RIASVLRIGV VGLMVAAMVV
     GTSRSEWPQQ IVLIGVYAVA ALWALLLAYS ASRRFFALRR FRSMGRLEPF AFTAVDVLIL
     TGFQLLSTDG IYPLLIMILL PVLVGLDVST RRAAVVLACT LVGFAVAVLG DPVMLRAIGW
     PETIFRFALY AFLCATALMV VRIEERHTRS VAGLSALRAE LLAQTMTASE VLQRRIAEAI
     HDGPLQDVLA ARQELIELDA VTPGDERVGR ALAGLQSASE RLRQATFELH PAVLEQVGLG
     PAVKQLAAST AQRSGIKIST DIDYPIRSGI DPIVFGVVRE LLSNVVRHSG ATTASVRLGI
     TDEKCVLDVA DDGVGVTGDT MARRLGEGHI GLASHRARVD AAGGVLVFLA TPRGTHVCVE
     LPLKR