MTRA_MYCS2
ID MTRA_MYCS2 Reviewed; 228 AA.
AC A0QTK2; I7FYZ5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=DNA-binding response regulator MtrA;
GN Name=mtrA; OrderedLocusNames=MSMEG_1874, MSMEI_1835;
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 PROBABLE FUNCTION, SUBUNIT, PHOSPHORYLATION, AND MUTAGENESIS OF ASP-56.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=20233304; DOI=10.1111/j.1365-2958.2010.07110.x;
RA Nguyen H.T., Wolff K.A., Cartabuke R.H., Ogwang S., Nguyen L.;
RT "A lipoprotein modulates activity of the MtrAB two-component system to
RT provide intrinsic multidrug resistance, cytokinetic control and cell wall
RT homeostasis in Mycobacterium.";
RL Mol. Microbiol. 76:348-364(2010).
CC -!- FUNCTION: Member of the two-component regulatory system MtrA/MtrB,
CC responding to environmental signals (Probable). Controls expression of
CC a number of genes including dnaA, ripA, fbpB and probably itself.
CC Probably plays a role in cell division. {ECO:0000305}.
CC -!- SUBUNIT: Probably a monomer when inactive, phosphorylation may permit
CC it to oligomerize (By similarity). The monomeric form does not seem to
CC be phosphorylated. {ECO:0000250, ECO:0000269|PubMed:20233304}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated by MtrB. {ECO:0000305|PubMed:20233304}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP38307.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK69775.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38307.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011727971.1; NZ_SIJM01000020.1.
DR RefSeq; YP_886240.1; NC_008596.1.
DR AlphaFoldDB; A0QTK2; -.
DR SMR; A0QTK2; -.
DR STRING; 246196.MSMEI_1835; -.
DR PRIDE; A0QTK2; -.
DR EnsemblBacteria; ABK69775; ABK69775; MSMEG_1874.
DR EnsemblBacteria; AFP38307; AFP38307; MSMEI_1835.
DR GeneID; 66733310; -.
DR KEGG; msg:MSMEI_1835; -.
DR KEGG; msm:MSMEG_1874; -.
DR PATRIC; fig|246196.19.peg.1856; -.
DR eggNOG; COG0745; Bacteria.
DR OMA; NIHGEGF; -.
DR OrthoDB; 817710at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..228
FT /note="DNA-binding response regulator MtrA"
FT /id="PRO_0000421122"
FT DOMAIN 7..120
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 128..227
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 56
FT /note="D->A: Does not complement an lpqB disruption mutant,
FT when overexpressed causes the same symptoms as an lpqB
FT disruption (antibiotic sensitivity, defects in cell
FT morphology and biofilm formation)."
FT /evidence="ECO:0000269|PubMed:20233304"
FT MUTAGEN 56
FT /note="D->E: Complements an lpqB disruption mutant, when
FT overexpressed restores biofilm formation to the lpqB
FT disruption. Acts like a dominant negative to wild-type."
FT /evidence="ECO:0000269|PubMed:20233304"
SQ SEQUENCE 228 AA; 25318 MW; FA45C9E560D4B4CC CRC64;
MDTMRQRILV VDDDPSLAEM LTIVLRGEGF DTAVIGDGSQ ALTAVRELRP DLVLLDLMLP
GMNGIDVCRV LRADSGVPIV MLTAKTDTVD VVLGLESGAD DYVMKPFKPK ELVARVRARL
RRNEDEPAEM LSIGDVEIDV PAHKVTRQGE QISLTPLEFD LLVALARKPR QVFTRDVLLE
QVWGYRHPAD TRLVNVHVQR LRAKVEKDPE NPQVVLTVRG VGYKAGPP
