PG16_MYCTU
ID PG16_MYCTU Reviewed; 923 AA.
AC Q79FU3; I6Y997; L0T5G5;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=PE-PGRS family protein PE_PGRS16 {ECO:0000305};
GN Name=PE_PGRS16 {ECO:0000312|EMBL:CCP43726.1};
GN OrderedLocusNames=Rv0977 {ECO:0000312|EMBL:CCP43726.1};
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 INDUCTION.
RX PubMed=16672626; DOI=10.1128/jb.188.10.3721-3725.2006;
RA Dheenadhayalan V., Delogu G., Sanguinetti M., Fadda G., Brennan M.J.;
RT "Variable expression patterns of Mycobacterium tuberculosis PE_PGRS genes:
RT evidence that PE_PGRS16 and PE_PGRS26 are inversely regulated in vivo.";
RL J. Bacteriol. 188:3721-3725(2006).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16586367; DOI=10.1086/502631;
RA Jain S.K., Paul-Satyaseela M., Lamichhane G., Kim K.S., Bishai W.R.;
RT "Mycobacterium tuberculosis invasion and traversal across an in vitro human
RT blood-brain barrier as a pathogenic mechanism for central nervous system
RT tuberculosis.";
RL J. Infect. Dis. 193:1287-1295(2006).
RN [4]
RP SUBCELLULAR LOCATION, AND EXPRESSION IN M.SMEGMATIS.
RX PubMed=18957600; DOI=10.1099/mic.0.2008/019968-0;
RA Singh P.P., Parra M., Cadieux N., Brennan M.J.;
RT "A comparative study of host response to three Mycobacterium tuberculosis
RT PE_PGRS proteins.";
RL Microbiology 154:3469-3479(2008).
RN [5] {ECO:0007744|PDB:4EHC}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 651-923 IN COMPLEX WITH ZINC, AND
RP DOMAIN.
RX PubMed=23923105; DOI=10.1016/j.fob.2013.05.004;
RA Barathy D.V., Suguna K.;
RT "Crystal structure of a putative aspartic proteinase domain of the
RT Mycobacterium tuberculosis cell surface antigen PE_PGRS16.";
RL FEBS Open Bio 3:256-262(2013).
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:18957600}.
CC -!- INDUCTION: Expression is induced in macrophages and infected mice
CC (PubMed:16672626). Highly up-regulated during the early stages of
CC invasion of the human blood-brain barrier (PubMed:16586367).
CC {ECO:0000269|PubMed:16586367, ECO:0000269|PubMed:16672626}.
CC -!- DOMAIN: Contains an aspartic proteinase-like domain in the C-terminal
CC region. However, the enzyme is inactive. A comparison of the structure
CC with pepsins showed significant differences in the critical substrate
CC binding residues and in the flap tyrosine conformation that could
CC contribute to the lack of proteolytic activity of PE_PGRS16.
CC {ECO:0000269|PubMed:23923105}.
CC -!- MISCELLANEOUS: Expression of this gene in M.smegmatis leads to
CC increased levels of NO and IL-12 and poor survival of recombinant
CC strains in macrophages. {ECO:0000269|PubMed:18957600}.
CC -!- MISCELLANEOUS: Contains a tightly bound zinc ion. The presence of this
CC ion is unexpected, and two His residues from the hexahistidine tag on
CC the expression vector contribute to the zinc binding site.
CC {ECO:0000269|PubMed:23923105}.
CC -!- SIMILARITY: Belongs to the mycobacterial PE family. PGRS subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP43726.1; -; Genomic_DNA.
DR RefSeq; WP_010886098.1; NZ_KK339370.1.
DR RefSeq; YP_177773.1; NC_000962.3.
DR PDB; 4EHC; X-ray; 1.98 A; A=651-923.
DR PDBsum; 4EHC; -.
DR AlphaFoldDB; Q79FU3; -.
DR SMR; Q79FU3; -.
DR STRING; 83332.Rv0977; -.
DR PaxDb; Q79FU3; -.
DR GeneID; 885264; -.
DR KEGG; mtu:Rv0977; -.
DR PATRIC; fig|83332.111.peg.1084; -.
DR TubercuList; Rv0977; -.
DR eggNOG; COG0657; Bacteria.
DR OMA; GAGNDIC; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR000084; PE-PGRS_N.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR Pfam; PF00934; PE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..923
FT /note="PE-PGRS family protein PE_PGRS16"
FT /id="PRO_0000438172"
FT DOMAIN 1..91
FT /note="PE"
FT /evidence="ECO:0000255"
FT REGION 121..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..923
FT /note="Aspartic proteinase-like domain"
FT /evidence="ECO:0000305|PubMed:23923105"
FT MOTIF 686..688
FT /note="D(T/S)G 1"
FT /evidence="ECO:0000305|PubMed:23923105"
FT MOTIF 839..841
FT /note="D(T/S)G 2"
FT /evidence="ECO:0000305|PubMed:23923105"
FT BINDING 686
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:23923105,
FT ECO:0007744|PDB:4EHC"
FT BINDING 839
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:23923105,
FT ECO:0007744|PDB:4EHC"
FT STRAND 657..660
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:4EHC"
FT TURN 665..667
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 668..675
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 681..686
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 690..694
FT /evidence="ECO:0007829|PDB:4EHC"
FT HELIX 696..700
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 708..714
FT /evidence="ECO:0007829|PDB:4EHC"
FT TURN 715..717
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 718..727
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 739..751
FT /evidence="ECO:0007829|PDB:4EHC"
FT HELIX 753..756
FT /evidence="ECO:0007829|PDB:4EHC"
FT TURN 757..760
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 763..768
FT /evidence="ECO:0007829|PDB:4EHC"
FT HELIX 780..783
FT /evidence="ECO:0007829|PDB:4EHC"
FT HELIX 786..790
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 791..795
FT /evidence="ECO:0007829|PDB:4EHC"
FT TURN 796..799
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 800..805
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 808..826
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 832..837
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:4EHC"
FT HELIX 849..852
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 865..870
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 875..881
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 889..894
FT /evidence="ECO:0007829|PDB:4EHC"
FT HELIX 901..905
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 908..911
FT /evidence="ECO:0007829|PDB:4EHC"
FT STRAND 918..920
FT /evidence="ECO:0007829|PDB:4EHC"
SQ SEQUENCE 923 AA; 81604 MW; 036E208B6E48C033 CRC64;
MSFVVTAPPV LASAASDLGG IASMISEANA MAAVRTTALA PAAADEVSAA IAALFSSYAR
DYQTLSVQVT AFHVQFAQTL TNAGQLYAVV DVGNGVLLKT EQQVLGVINA PTQTLVGRPL
IGDGTHGAPG TGQNGGAGGI LWGNGGNGGS GAPGQPGGRG GDAGLFGHGG HGGVGGPGIA
GAAGTAGLPG GNGANGGSGG IGGAGGAGGN GGLLFGNGGA GGQGGSGGLG GSGGTGGAGM
AAGPAGGTGG IGGIGGIGGA GGVGGHGSAL FGHGGINGDG GTGGMGGQGG AGGNGWAAEG
ITVGIGEQGG QGGDGGAGGA GGIGGSAGGI GGSQGAGGHG GDGGQGGAGG SGGVGGGGAG
AGGDGGAGGI GGTGGNGSIG GAAGNGGNGG RGGAGGMATA GSDGGNGGGG GNGGVGVGSA
GGAGGTGGDG GAAGAGGAPG HGYFQQPAPQ GLPIGTGGTG GEGGAGGAGG DGGQGDIGFD
GGRGGDGGPG GGGGAGGDGS GTFNAQANNG GDGGAGGVGG AGGTGGTGGV GADGGRGGDS
GRGGDGGNAG HGGAAQFSGR GAYGGEGGSG GAGGNAGGAG TGGTAGSGGA GGFGGNGADG
GNGGNGGNGG FGGINGTFGT NGAGGTGGLG TLLGGHNGNI GLNGATGGIG STTLTNATVP
LQLVNTTEPV VFISLNGGQM VPVLLDTGST GLVMDSQFLT QNFGPVIGTG TAGYAGGLTY
NYNTYSTTVD FGNGLLTLPT SVNVVTSSSP GTLGNFLSRS GAVGVLGIGP NNGFPGTSSI
VTAMPGLLNN GVLIDESAGI LQFGPNTLTG GITISGAPIS TVAVQIDNGP LQQAPVMFDS
GGINGTIPSA LASLPSGGFV PAGTTISVYT SDGQTLLYSY TTTATNTPFV TSGGVMNTGH
VPFAQQPIYV SYSPTAIGTT TFN
