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Database: UniProt
Entry: KDPE_MYCTU
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ID   KDPE_MYCTU              Reviewed;         226 AA.
AC   P9WGN1; L0T8E7; P96373; Q7D8Z1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Transcriptional regulatory protein KdpE;
GN   Name=kdpE; OrderedLocusNames=Rv1027c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=12595424; DOI=10.1128/iai.71.3.1134-1140.2003;
RA   Parish T., Smith D.A., Kendall S., Casali N., Bancroft G.J., Stoker N.G.;
RT   "Deletion of two-component regulatory systems increases the virulence of
RT   Mycobacterium tuberculosis.";
RL   Infect. Immun. 71:1134-1140(2003).
RN   [3]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011445;
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   [5]
RP   FUNCTION, PHOSPHORYLATION AT ASP-52, AND MUTAGENESIS OF ASP-52.
RX   PubMed=24667597; DOI=10.1016/j.bbrc.2014.03.066;
RA   Agrawal R., Saini D.K.;
RT   "Rv1027c-Rv1028c encode functional KdpDE two--component system in
RT   Mycobacterium tuberculosis.";
RL   Biochem. Biophys. Res. Commun. 446:1172-1178(2014).
CC   -!- FUNCTION: Member of the two-component regulatory system KdpD/KdpE
CC       involved in the regulation of the kdp operon. Upon phosphorylation by
CC       KdpD, functions as a transcription regulator by direct binding to
CC       promoter regions of target genes to positively regulate their
CC       expression. {ECO:0000269|PubMed:24667597}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylated by KdpD. {ECO:0000269|PubMed:24667597}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking KdpD and KdpE show an increase in
CC       virulence in mouse model of infection, with significantly shorter
CC       survival times. {ECO:0000269|PubMed:12595424}.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
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DR   EMBL; AL123456; CCP43777.1; -; Genomic_DNA.
DR   PIR; F70623; F70623.
DR   RefSeq; NP_215543.1; NC_000962.3.
DR   RefSeq; WP_003405305.1; NZ_NVQJ01000018.1.
DR   AlphaFoldDB; P9WGN1; -.
DR   SMR; P9WGN1; -.
DR   IntAct; P9WGN1; 1.
DR   STRING; 83332.Rv1027c; -.
DR   PaxDb; 83332-Rv1027c; -.
DR   DNASU; 886046; -.
DR   GeneID; 45424999; -.
DR   GeneID; 886046; -.
DR   KEGG; mtu:Rv1027c; -.
DR   TubercuList; Rv1027c; -.
DR   eggNOG; COG0745; Bacteria.
DR   InParanoid; P9WGN1; -.
DR   OrthoDB; 9790442at2; -.
DR   PhylomeDB; P9WGN1; -.
DR   PHI-base; PHI:3619; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd17620; REC_OmpR_KdpE-like; 1.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.250.690; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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:SF50; KDP OPERON TRANSCRIPTIONAL REGULATORY PROTEIN KDPE; 1.
DR   PANTHER; PTHR48111; REGULATOR OF RPOS; 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; CheY-like; 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..226
FT                   /note="Transcriptional regulatory protein KdpE"
FT                   /id="PRO_0000412199"
FT   DOMAIN          3..116
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        127..226
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT   MOD_RES         52
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT                   ECO:0000269|PubMed:24667597"
FT   MUTAGEN         52
FT                   /note="D->N: Complete loss of phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:24667597"
SQ   SEQUENCE   226 AA;  24741 MW;  68BE8DDC38AED423 CRC64;
     MTLVLVIDDE PQILRALRIN LTVRGYQVIT ASTGAGALRA AAEHPPDVVI LDLGLPDMSG
     IDVLGGLRGW LTAPVIVLSA RTDSSDKVQA LDAGADDYVT KPFGMDEFLA RLRAAVRRNT
     AAAELEQPVI ETDSFTVDLA GKKVIKDGAE VHLTPTEWGM LEMLARNRGK LVGRGELLKE
     VWGPAYATET HYLRVYLAQL RRKLEDDPSH PKHLLTESGM GYRFEA
//
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