ID   MTRB_MYCS2              Reviewed;         553 AA.
AC   A0QTK3; I7FHM1;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Sensor histidine kinase MtrB;
DE            EC=2.7.13.3;
GN   Name=mtrB; OrderedLocusNames=MSMEG_1875, MSMEI_1836;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
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.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=22610443; DOI=10.1074/jbc.m112.346544;
RA   Plocinska R., Purushotham G., Sarva K., Vadrevu I.S., Pandeeti E.V.,
RA   Arora N., Plocinski P., Madiraju M.V., Rajagopalan M.;
RT   "Septal localization of the Mycobacterium tuberculosis MtrB sensor kinase
RT   promotes MtrA regulon expression.";
RL   J. Biol. Chem. 287:23887-23899(2012).
CC   -!- FUNCTION: Member of the two-component regulatory system MtrA/MtrB.
CC       Probably functions as a membrane-associated protein kinase that
CC       phosphorylates MtrA in response to environmental signals (By
CC       similarity). MtrB may be active only at septa where it promotes MtrA
CC       phosphorylation and MtrA regulon expression, probably playing a role in
CC       cell division. {ECO:0000250, ECO:0000269|PubMed:22610443}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBUNIT: Interacts with MrtA. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22610443};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:22610443}. Note=Found
CC       at the septa or mid-cell; correct localization requires correct FtsZ
CC       localization.
CC   -!- DISRUPTION PHENOTYPE: Grows poorly with filamentous cells, often with
CC       bulbous regions and a chain-like phenotype indicating possible defects
CC       in septum splitting and cell wall metabolism. Increased sensitivity to
CC       lysozyme. Decreased expression of the MtrA/MtrB regulon genes dnaA,
CC       ripA, and fbpB. {ECO:0000269|PubMed:22610443}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK75150.1; 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; CP000480; ABK75150.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001663; AFP38308.1; -; Genomic_DNA.
DR   RefSeq; WP_014877234.1; NZ_SIJM01000020.1.
DR   RefSeq; YP_886241.1; NC_008596.1.
DR   AlphaFoldDB; A0QTK3; -.
DR   SMR; A0QTK3; -.
DR   STRING; 246196.MSMEI_1836; -.
DR   PRIDE; A0QTK3; -.
DR   EnsemblBacteria; ABK75150; ABK75150; MSMEG_1875.
DR   EnsemblBacteria; AFP38308; AFP38308; MSMEI_1836.
DR   GeneID; 66733311; -.
DR   KEGG; msg:MSMEI_1836; -.
DR   KEGG; msm:MSMEG_1875; -.
DR   PATRIC; fig|246196.19.peg.1857; -.
DR   eggNOG; COG5002; Bacteria.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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..553
FT                   /note="Sensor histidine kinase MtrB"
FT                   /id="PRO_0000421123"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          234..286
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          301..518
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          523..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         304
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   553 AA;  60233 MW;  4EF6F34D5571C136 CRC64;
     MIFGSRRRIR GRWGGSGPLV RGLGTLGRAL SLVWRRSLQL RVVTLTLGLS LAVILVLGFV
     LTSQITDRIL EVKVKAATEE VERARNTVSG IVGGEESRSL ESSLQLARNT LVDRKADVRA
     DMAGAFDAVL VVPGDGPRAA AAAGPVAQIP EALRDFVKAG QVSYQYATVQ TEGFSGPALI
     VGSPTTSSVP NLELYLIFPL NNEESTIALV RGTMATGGVV LLGLLAAIAL VVARQIVQPV
     RSASRIAERF AEGHLTERMP VRGEDDMARL AVSFNDMAES LSRQIQQLEE FGNLQRRFTS
     DVSHELRTPL TTVRMAADLI YDHSEDLDPA LRRSTELMVN ELDRFETLLA DLLEISRHDA
     GVAELSVESL DLRSTVRSAL DNVGHLAADA GVELTLDMPE EDVIAEVDPR RVERILRNLI
     ANAIDHAESK PVQIRMAADE DTVAVTVRDF GVGLRPGEEK LVFSRFWRSD PSRVRRSGGT
     GLGLAISIED ARLHQGRLEA WGEPGKGACF RLTLPLVRGH KVTTSPLPLK PASEQRPARR
     RSNKDREAAE ESV