ID   MCTS_RHIL3              Reviewed;         461 AA.
AC   Q1M799; Q8VM89;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Sensor histidine kinase MctS {ECO:0000305};
DE            EC=2.7.13.3 {ECO:0000250};
GN   Name=mctS {ECO:0000303|PubMed:12218032};
GN   OrderedLocusNames=pRL100407 {ECO:0000312|EMBL:CAK10633.1};
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OG   Plasmid pRL10 {ECO:0000312|EMBL:CAK10633.1}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=3841;
RX   PubMed=12218032; DOI=10.1128/jb.184.19.5436-5448.2002;
RA   Hosie A.H., Allaway D., Poole P.S.;
RT   "A monocarboxylate permease of Rhizobium leguminosarum is the first member
RT   of a new subfamily of transporters.";
RL   J. Bacteriol. 184:5436-5448(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
CC   -!- FUNCTION: Member of the two-component regulatory system MctS/MctR,
CC       which activates mctP expression. {ECO:0000269|PubMed:12218032}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD19126.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ421944; CAD19126.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AM236084; CAK10633.1; -; Genomic_DNA.
DR   RefSeq; WP_011654431.1; NC_008381.1.
DR   AlphaFoldDB; Q1M799; -.
DR   SMR; Q1M799; -.
DR   EnsemblBacteria; CAK10633; CAK10633; pRL100407.
DR   KEGG; rle:pRL100407; -.
DR   HOGENOM; CLU_000445_20_6_5; -.
DR   OMA; RNLMHPR; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000006575; Plasmid pRL10.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR033480; sCache_2.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR017171; Sig_transdc_His_kinase_MctS.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF17200; sCache_2; 1.
DR   PIRSF; PIRSF037314; STHK_MctS; 1.
DR   SMART; SM01049; Cache_2; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Plasmid; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..461
FT                   /note="Sensor histidine kinase MctS"
FT                   /id="PRO_0000430568"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          360..450
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         259
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   461 AA;  50713 MW;  64F160DBCB15189B CRC64;
     MTLRHQIIAL AIVPLVISIL AITTFITWQS ANLAKNSIDT FEQNMLKTKE AEILNLTNLA
     LSAIQTIYDK AGSDDEAAKQ QVAAILTSLD YGKDGYFFVY DYDGNNIVHP RQSFRHGHNW
     LDLTDPDGDK VIAELIATAK AGGGLHQYKW QKPSTGQIAD KLSFVVSLDK WHWVVGTGVY
     LDDVFAQSAA ANAGMRANIK RTFVIVALID VPSVLVVFTT CMLLTFHERR MADSRLKALT
     QRVIDTQEEE RARLARELHD GISQNLVGVR YAMDLAGRKV RTNVDDAALT IDRGVEALNG
     AIKEIRRLSH DLRPRVLDDL GLTAALEALC YHFAERTGIE TKIDASGFTD TLKAEANTAL
     YRVAQEAFNN VERHAGASKL AVKLWSDNGR ARMTVSDNGA GFDGIKDGMS GRSGLGLRNM
     QERMAHFRGL LLINSSEAGT TLTAMMPKSA NRPVNRQAEA A