EMBR_MYCTU
ID EMBR_MYCTU Reviewed; 388 AA.
AC P9WGJ9; L0T949; P66799; Q11052;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Transcriptional regulatory protein EmbR;
GN Name=embR; OrderedLocusNames=Rv1267c; ORFNames=MTCY50.15;
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 PHOSPHORYLATION, AND MUTAGENESIS OF ARG-312; SER-326 AND ASN-348.
RX PubMed=14690440; DOI=10.1021/bi035150b;
RA Molle V., Kremer L., Girard-Blanc C., Besra G.S., Cozzone A.J., Prost J.F.;
RT "An FHA phosphoprotein recognition domain mediates protein EmbR
RT phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium
RT tuberculosis.";
RL Biochemistry 42:15300-15309(2003).
RN [3]
RP FUNCTION, INTERACTION WITH RNA POLYMERASE, PHOSPHORYLATION, AND
RP DEPHOSPHORYLATION.
RX PubMed=16817899; DOI=10.1111/j.1742-4658.2006.05289.x;
RA Sharma K., Gupta M., Krupa A., Srinivasan N., Singh Y.;
RT "EmbR, a regulatory protein with ATPase activity, is a substrate of
RT multiple serine/threonine kinases and phosphatase in Mycobacterium
RT tuberculosis.";
RL FEBS J. 273:2711-2721(2006).
RN [4]
RP FUNCTION, DNA-BINDING, AND PHOSPHORYLATION.
RX PubMed=16585755; DOI=10.1128/jb.188.8.2936-2944.2006;
RA Sharma K., Gupta M., Pathak M., Gupta N., Koul A., Sarangi S., Baweja R.,
RA Singh Y.;
RT "Transcriptional control of the mycobacterial embCAB operon by PknH through
RT a regulatory protein, EmbR, in vivo.";
RL J. Bacteriol. 188:2936-2944(2006).
RN [5]
RP PHOSPHORYLATION, AND MUTAGENESIS OF THR-209.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17286964; DOI=10.1016/j.bbrc.2007.01.122;
RA Zheng X., Papavinasasundaram K.G., Av-Gay Y.;
RT "Novel substrates of Mycobacterium tuberculosis PknH Ser/Thr kinase.";
RL Biochem. Biophys. Res. Commun. 355:162-168(2007).
RN [6]
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 [7]
RP SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=32634279; DOI=10.1111/mmi.14571;
RA Zaveri A., Wang R., Botella L., Sharma R., Zhu L., Wallach J.B., Song N.,
RA Jansen R.S., Rhee K.Y., Ehrt S., Schnappinger D.;
RT "Depletion of the DarG antitoxin in Mycobacterium tuberculosis triggers the
RT DNA-damage response and leads to cell death.";
RL Mol. Microbiol. 114:641-652(2020).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND DOMAIN.
RX PubMed=16477027; DOI=10.1073/pnas.0507766103;
RA Alderwick L.J., Molle V., Kremer L., Cozzone A.J., Dafforn T.R.,
RA Besra G.S., Futterer K.;
RT "Molecular structure of EmbR, a response element of Ser/Thr kinase
RT signaling in Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2558-2563(2006).
CC -!- FUNCTION: Positively regulates the transcription of the embCAB operon.
CC Exhibits ATPase and GTPase activities. {ECO:0000269|PubMed:16585755,
CC ECO:0000269|PubMed:16817899}.
CC -!- SUBUNIT: Interacts with RNA polymerase (PubMed:16817899). Co-
CC immunoprecipitates with DarG in the presence and absence of darT
CC (PubMed:32634279). {ECO:0000269|PubMed:16817899,
CC ECO:0000269|PubMed:32634279}.
CC -!- DOMAIN: Contains a N-terminal winged-helix DNA-binding domain and a
CC regulatory C-terminal forkhead-associated (FHA) domain, which mediates
CC binding to a Thr-phosphorylated site in the cognate kinase.
CC {ECO:0000269|PubMed:16477027}.
CC -!- PTM: Phosphorylated on threonine residue(s) by PknH, PknA and PknB.
CC Phosphorylation enhances the DNA-binding activity of EmbR.
CC Dephosphorylated by PstP. {ECO:0000269|PubMed:14690440,
CC ECO:0000269|PubMed:16585755, ECO:0000269|PubMed:16817899,
CC ECO:0000269|PubMed:17286964}.
CC -!- SIMILARITY: Belongs to the AfsR/DnrI/RedD regulatory family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44023.1; -; Genomic_DNA.
DR PIR; C70754; C70754.
DR RefSeq; NP_215783.1; NC_000962.3.
DR RefSeq; WP_003406553.1; NZ_NVQJ01000030.1.
DR PDB; 2FEZ; X-ray; 2.00 A; A=1-388.
DR PDB; 2FF4; X-ray; 1.90 A; A/B=1-388.
DR PDBsum; 2FEZ; -.
DR PDBsum; 2FF4; -.
DR AlphaFoldDB; P9WGJ9; -.
DR SMR; P9WGJ9; -.
DR IntAct; P9WGJ9; 1.
DR STRING; 83332.Rv1267c; -.
DR PaxDb; P9WGJ9; -.
DR DNASU; 887026; -.
DR GeneID; 45425239; -.
DR GeneID; 887026; -.
DR KEGG; mtu:Rv1267c; -.
DR TubercuList; Rv1267c; -.
DR eggNOG; COG1716; Bacteria.
DR eggNOG; COG3629; Bacteria.
DR OMA; QFVDAFA; -.
DR PhylomeDB; P9WGJ9; -.
DR SABIO-RK; P9WGJ9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0003924; F:GTPase activity; IDA:MTBBASE.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MTBBASE.
DR CDD; cd15831; BTAD; 1.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR005158; BTAD.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF03704; BTAD; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM01043; BTAD; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..388
FT /note="Transcriptional regulatory protein EmbR"
FT /id="PRO_0000110008"
FT DOMAIN 308..357
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DNA_BIND 2..105
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MUTAGEN 209
FT /note="T->A: Decreases phosphorylation by PknH."
FT /evidence="ECO:0000269|PubMed:17286964"
FT MUTAGEN 312
FT /note="R->A: Abolished phosphorylation."
FT /evidence="ECO:0000269|PubMed:14690440"
FT MUTAGEN 326
FT /note="S->A: Abolished phosphorylation."
FT /evidence="ECO:0000269|PubMed:14690440"
FT MUTAGEN 348
FT /note="N->A: Abolished phosphorylation."
FT /evidence="ECO:0000269|PubMed:14690440"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:2FF4"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 159..183
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 205..216
FT /evidence="ECO:0007829|PDB:2FF4"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 221..239
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:2FF4"
FT HELIX 262..280
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:2FF4"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:2FF4"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:2FF4"
SQ SEQUENCE 388 AA; 41933 MW; 8221B6EAF1C33354 CRC64;
MAGSATVEKR LDFGLLGPLQ MTIDGTPVPS GTPKQRAVLA MLVINRNRPV GVDALITALW
EEWPPSGARA SIHSYVSNLR KLLGGAGIDP RVVLAAAPPG YRLSIPDNTC DLGRFVAEKT
AGVHAAAAGR FEQASRHLSA ALREWRGPVL DDLRDFQFVE PFATALVEDK VLAHTAKAEA
EIACGRASAV IAELEALTFE HPYREPLWTQ LITAYYLSDR QSDALGAYRR VKTTLADDLG
IDPGPTLRAL NERILRQQPL DAKKSAKTTA AGTVTVLDQR TMASGQQAVA YLHDIASGRG
YPLQAAATRI GRLHDNDIVL DSANVSRHHA VIVDTGTNYV INDLRSSNGV HVQHERIRSA
VTLNDGDHIR ICDHEFTFQI SAGTHGGT
