ID   MTRB_MYCLE              Reviewed;         562 AA.
AC   Q9CCJ1;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Sensor histidine kinase MtrB;
DE            EC=2.7.13.3;
GN   Name=mtrB; OrderedLocusNames=ML0774;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Member of the two-component regulatory system MtrA/MtrB.
CC       Seems to function as a membrane-associated protein kinase that
CC       phosphorylates MtrA in response to environmental signals (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AL583919; CAC30283.1; -; Genomic_DNA.
DR   PIR; G87005; G87005.
DR   RefSeq; NP_301598.1; NC_002677.1.
DR   RefSeq; WP_010907922.1; NC_002677.1.
DR   AlphaFoldDB; Q9CCJ1; -.
DR   SMR; Q9CCJ1; -.
DR   STRING; 272631.ML0774; -.
DR   PRIDE; Q9CCJ1; -.
DR   EnsemblBacteria; CAC30283; CAC30283; CAC30283.
DR   KEGG; mle:ML0774; -.
DR   PATRIC; fig|272631.5.peg.1392; -.
DR   Leproma; ML0774; -.
DR   eggNOG; COG5000; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_18_11; -.
DR   OMA; NRFWRSD; -.
DR   Proteomes; UP000000806; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 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   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; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..562
FT                   /note="Sensor histidine kinase MtrB"
FT                   /id="PRO_0000074807"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          235..287
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          302..519
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          526..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   562 AA;  61506 MW;  741EB0087AEC155E CRC64;
     MIFSSRRRIR GRWGRSGPMM RGMGALTRVV GVVWRRSLQL RVVALTFGLS LAVILALGFV
     LTSQLTSRVL DVKVRVAIEQ IERARTTVTG IVNGEETRSL DSSLQLARNT LTSKTDPTSG
     AGLVGAFDAV LIVPGDGPRT ATTAGPVDQV PNSLRGFIKA GQAAYQYATV HTEGFSGPAL
     IIGTPTSSQV TNLELYLIFP LKNEQATVTL VRGTMATGGM VLLVLLSGIA LLVSRQVVVP
     VRSASRIAER FAEGHLSERM PVRGEDDMAR LAVSFNDMAE SLSRQITQLE EFGNLQRRFT
     SDVSHELRTP LTTVRMAADL IYDHSSDLDP TLRRSTELMV SELDRFETLL NDLLEISRHD
     AGVAELSVEA VDLRVMVNNA LGNVGHLAEE AGIELLVDMP VDEVIAEVDA RRVERILRNL
     IANAIDHSEH KPVRIRMAAD EDTVAVTVRD YGIGLRPGEE KLVFSRFWRS DPSRVRRSGG
     TGLGLAISIE DARLHQGRLE AWGEPGQGAC FRLTLPLVRG HKVTTSPLPM KPILQPSPQA
     STAGQQHGTQ RQRLREHAER SR