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PE25_MYCTU
ID   PE25_MYCTU              Reviewed;          99 AA.
AC   I6X486;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=PE-PGRS family protein PE25 {ECO:0000305};
GN   Name=PE25 {ECO:0000312|EMBL:CCP45223.1};
GN   OrderedLocusNames=Rv2431c {ECO:0000312|EMBL:CCP45223.1};
GN   ORFNames=LH57_13295 {ECO:0000312|EMBL:AIR15198.1};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA   Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA   Monaco A., King S., Sohrabi A.;
RT   "Phylogenetic analysis of Mycobacterial species using whole genome
RT   sequences.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=18974870; DOI=10.1371/journal.pone.0003586;
RA   Tundup S., Pathak N., Ramanadham M., Mukhopadhyay S., Murthy K.J.,
RA   Ehtesham N.Z., Hasnain S.E.;
RT   "The co-operonic PE25/PPE41 protein complex of Mycobacterium tuberculosis
RT   elicits increased humoral and cell mediated immune response.";
RL   PLoS ONE 3:E3586-E3586(2008).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [5]
RP   FUNCTION.
RX   PubMed=25379378; DOI=10.1016/j.fob.2014.09.001;
RA   Tundup S., Mohareer K., Hasnain S.E.;
RT   "Mycobacterium tuberculosis PE25/PPE41 protein complex induces necrosis in
RT   macrophages: Role in virulence and disease reactivation?";
RL   FEBS Open Bio 4:822-828(2014).
RN   [6]
RP   FUNCTION.
RC   STRAIN=H37Rv;
RX   PubMed=26318856; DOI=10.1007/s00430-015-0434-x;
RA   Chen W., Bao Y., Chen X., Burton J., Gong X., Gu D., Mi Y., Bao L.;
RT   "Mycobacterium tuberculosis PE25/PPE41 protein complex induces activation
RT   and maturation of dendritic cells and drives Th2-biased immune responses.";
RL   Med. Microbiol. Immunol. 205:119-131(2016).
RN   [7] {ECO:0007744|PDB:2G38}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH PPE41, AND SUBUNIT.
RC   STRAIN=H37Rv;
RX   PubMed=16690741; DOI=10.1073/pnas.0602606103;
RA   Strong M., Sawaya M.R., Wang S., Phillips M., Cascio D., Eisenberg D.;
RT   "Toward the structural genomics of complexes: crystal structure of a PE/PPE
RT   protein complex from Mycobacterium tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:8060-8065(2006).
RN   [8] {ECO:0007744|PDB:4KXR}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH PPE41 AND ESPG5, AND
RP   SUBUNIT.
RX   PubMed=25155747; DOI=10.1111/mmi.12770;
RA   Korotkova N., Freire D., Phan T.H., Ummels R., Creekmore C.C., Evans T.J.,
RA   Wilmanns M., Bitter W., Parret A.H., Houben E.N., Korotkov K.V.;
RT   "Structure of the Mycobacterium tuberculosis type VII secretion system
RT   chaperone EspG5 in complex with PE25-PPE41 dimer.";
RL   Mol. Microbiol. 94:367-382(2014).
RN   [9] {ECO:0007744|PDB:4W4K, ECO:0007744|PDB:4W4L}
RP   X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH PPE41 AND IN COMPLEX
RP   WITH PPE41 AND ESPG5, AND SUBUNIT.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=25275011; DOI=10.1073/pnas.1409345111;
RA   Ekiert D.C., Cox J.S.;
RT   "Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals
RT   molecular specificity of ESX protein secretion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:14758-14763(2014).
CC   -!- FUNCTION: The PE25/PPE41 dimer induces both a strong humoral and
CC       cellular immune response. PE25 protein alone induces low response
CC       (PubMed:18974870). The dimer induces necrosis, but not apoptosis, in
CC       mouse macrophage cells (PubMed:25379378). It also induces activation
CC       and maturation of mouse dendritic cells and drives Th2-biased immune
CC       responses (PubMed:26318856). {ECO:0000269|PubMed:18974870,
CC       ECO:0000269|PubMed:25379378, ECO:0000269|PubMed:26318856}.
CC   -!- SUBUNIT: Forms a heterodimer with PPE41. The dimer forms a 1:1:1
CC       heterotrimeric complex with EspG5. {ECO:0000269|PubMed:16690741,
CC       ECO:0000269|PubMed:25155747, ECO:0000269|PubMed:25275011}.
CC   -!- INTERACTION:
CC       I6X486; Q79FE1: PPE41; NbExp=3; IntAct=EBI-15582196, EBI-8063017;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Secreted via the
CC       ESX-5 / type VII secretion system (T7SS). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the mycobacterial PE family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP45223.1; -; Genomic_DNA.
DR   EMBL; CP009480; AIR15198.1; -; Genomic_DNA.
DR   RefSeq; WP_003412551.1; NZ_NVQJ01000024.1.
DR   RefSeq; YP_177882.1; NC_000962.3.
DR   PDB; 2G38; X-ray; 2.20 A; A/C=1-99.
DR   PDB; 4KXR; X-ray; 2.60 A; A=1-99.
DR   PDB; 4W4K; X-ray; 1.95 A; A/C=6-99.
DR   PDB; 4W4L; X-ray; 2.45 A; A=1-99.
DR   PDB; 6VJ5; X-ray; 2.40 A; A=1-99.
DR   PDBsum; 2G38; -.
DR   PDBsum; 4KXR; -.
DR   PDBsum; 4W4K; -.
DR   PDBsum; 4W4L; -.
DR   PDBsum; 6VJ5; -.
DR   AlphaFoldDB; I6X486; -.
DR   SMR; I6X486; -.
DR   DIP; DIP-61169N; -.
DR   IntAct; I6X486; 1.
DR   STRING; 83332.Rv2431c; -.
DR   iPTMnet; I6X486; -.
DR   PaxDb; I6X486; -.
DR   PRIDE; I6X486; -.
DR   DNASU; 885703; -.
DR   GeneID; 45426421; -.
DR   GeneID; 885703; -.
DR   KEGG; mtu:Rv2431c; -.
DR   PATRIC; fig|83332.111.peg.2718; -.
DR   TubercuList; Rv2431c; -.
DR   HOGENOM; CLU_000167_16_11_11; -.
DR   PhylomeDB; I6X486; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000084; PE-PGRS_N.
DR   Pfam; PF00934; PE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Reference proteome; Secreted; Virulence.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   CHAIN           2..99
FT                   /note="PE-PGRS family protein PE25"
FT                   /id="PRO_0000435110"
FT   DOMAIN          1..92
FT                   /note="PE"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   HELIX           8..36
FT                   /evidence="ECO:0007829|PDB:6VJ5"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:6VJ5"
FT   HELIX           46..84
FT                   /evidence="ECO:0007829|PDB:6VJ5"
FT   TURN            85..87
FT                   /evidence="ECO:0007829|PDB:6VJ5"
SQ   SEQUENCE   99 AA;  10687 MW;  D931C0DB4265B3F9 CRC64;
     MSFVITNPEA LTVAATEVRR IRDRAIQSDA QVAPMTTAVR PPAADLVSEK AATFLVEYAR
     KYRQTIAAAA VVLEEFAHAL TTGADKYATA EADNIKTFS
 
 
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