RPFE_MYCTU
ID RPFE_MYCTU Reviewed; 172 AA.
AC O53177; L0TCD7;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Resuscitation-promoting factor RpfE;
DE EC=3.-.-.-;
DE Flags: Precursor;
GN Name=rpfE; OrderedLocusNames=Rv2450c; ORFNames=MTV008.06c;
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 FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12410821; DOI=10.1046/j.1365-2958.2002.03184.x;
RA Mukamolova G.V., Turapov O.A., Young D.I., Kaprelyants A.S., Kell D.B.,
RA Young M.;
RT "A family of autocrine growth factors in Mycobacterium tuberculosis.";
RL Mol. Microbiol. 46:623-635(2002).
RN [3]
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12874362; DOI=10.1128/iai.71.8.4789-4794.2003;
RA Yeremeev V.V., Kondratieva T.K., Rubakova E.I., Petrovskaya S.N.,
RA Kazarian K.A., Telkov M.V., Biketov S.F., Kaprelyants A.S., Apt A.S.;
RT "Proteins of the Rpf family: immune cell reactivity and vaccination
RT efficacy against tuberculosis in mice.";
RL Infect. Immun. 71:4789-4794(2003).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15207486; DOI=10.1016/j.tube.2003.12.004;
RA Downing K.J., Betts J.C., Young D.I., McAdam R.A., Kelly F., Young M.,
RA Mizrahi V.;
RT "Global expression profiling of strains harbouring null mutations reveals
RT that the five rpf-like genes of Mycobacterium tuberculosis show functional
RT redundancy.";
RL Tuberculosis 84:167-179(2004).
RN [5]
RP INTERACTION WITH RIPA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17919286; DOI=10.1111/j.1365-2958.2007.05945.x;
RA Hett E.C., Chao M.C., Steyn A.J., Fortune S.M., Deng L.L., Rubin E.J.;
RT "A partner for the resuscitation-promoting factors of Mycobacterium
RT tuberculosis.";
RL Mol. Microbiol. 66:658-668(2007).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18186793; DOI=10.1111/j.1365-2958.2007.06078.x;
RA Kana B.D., Gordhan B.G., Downing K.J., Sung N., Vostroktunova G.,
RA Machowski E.E., Tsenova L., Young M., Kaprelyants A., Kaplan G.,
RA Mizrahi V.;
RT "The resuscitation-promoting factors of Mycobacterium tuberculosis are
RT required for virulence and resuscitation from dormancy but are collectively
RT dispensable for growth in vitro.";
RL Mol. Microbiol. 67:672-684(2008).
CC -!- FUNCTION: Factor that stimulates resuscitation of dormant cells. Has
CC peptidoglycan (PG) hydrolytic activity. Active in the pM concentration
CC range. Has little to no effect on actively-growing cells. PG fragments
CC could either directly activate the resuscitation pathway of dormant
CC bacteria or serve as a substrate for endogenous Rpf, resulting in low
CC molecular weight products with resuscitation activity.
CC {ECO:0000269|PubMed:12410821}.
CC -!- FUNCTION: Stimulates growth of stationary phase M.bovis (a slow-growing
CC Mycobacterium), reduces the lag phase of diluted fast-growers
CC M.smegmatis and Micrococcus luteus. Sequential gene disruption
CC indicates RpfB and RpfE are higher than RpfD and RpfC in functional
CC hierarchy. {ECO:0000269|PubMed:12410821}.
CC -!- SUBUNIT: Interacts with RipA. {ECO:0000269|PubMed:17919286}.
CC -!- INDUCTION: Expressed in actively growing cells.
CC {ECO:0000269|PubMed:12410821}.
CC -!- DISRUPTION PHENOTYPE: Not essential, disruption of rpfE alone has no
CC effect on growth or survival in liquid culture, nor in mouse infection
CC models, although colony size is reduced. Alterations in gene expression
CC are seen. All 5 genes in this family can be deleted without affecting
CC growth in culture, however quadruple deletion mutants (rpfA-rpfC-rpfB-
CC rpfE or rpfA-rpfC-rpfD-rpfE) are not able to resuscitate spontaneously
CC in the presence or absence of O(2), and are attenuated in a mouse
CC infection model. {ECO:0000269|PubMed:15207486,
CC ECO:0000269|PubMed:18186793}.
CC -!- BIOTECHNOLOGY: Might be a good vaccine candidate.
CC {ECO:0000269|PubMed:12874362}.
CC -!- SIMILARITY: Belongs to the transglycosylase family. Rpf subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45243.1; -; Genomic_DNA.
DR PIR; A70864; A70864.
DR RefSeq; NP_216966.1; NC_000962.3.
DR RefSeq; WP_010886146.1; NC_000962.3.
DR PDB; 4CGE; X-ray; 2.76 A; A/B/C/D/E/F=98-172.
DR PDBsum; 4CGE; -.
DR AlphaFoldDB; O53177; -.
DR SMR; O53177; -.
DR STRING; 83332.Rv2450c; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR PaxDb; O53177; -.
DR GeneID; 885760; -.
DR KEGG; mtu:Rv2450c; -.
DR PATRIC; fig|83332.12.peg.2746; -.
DR TubercuList; Rv2450c; -.
DR eggNOG; COG1388; Bacteria.
DR OMA; KAYSVNW; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:MTBBASE.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MTBBASE.
DR GO; GO:0040010; P:positive regulation of growth rate; IDA:MTBBASE.
DR CDD; cd13925; RPF; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR010618; RPF.
DR Pfam; PF06737; Transglycosylas; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome; Signal; Virulence.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..172
FT /note="Resuscitation-promoting factor RpfE"
FT /id="PRO_0000421031"
FT REGION 33..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:4CGE"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4CGE"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:4CGE"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:4CGE"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:4CGE"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:4CGE"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4CGE"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:4CGE"
SQ SEQUENCE 172 AA; 17456 MW; 0D67E72240EF0F0E CRC64;
MKNARTTLIA AAIAGTLVTT SPAGIANADD AGLDPNAAAG PDAVGFDPNL PPAPDAAPVD
TPPAPEDAGF DPNLPPPLAP DFLSPPAEEA PPVPVAYSVN WDAIAQCESG GNWSINTGNG
YYGGLRFTAG TWRANGGSGS AANASREEQI RVAENVLRSQ GIRAWPVCGR RG
