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10 kDa chaperonin (10 kDa antigen) (BCG-A heat shock protein) (GroES protein) (Protein Cpn10)

 CH10_MYCTU              Reviewed;         100 AA.
P9WPE5; L0TFJ8; P09621;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
28-FEB-2018, entry version 31.
RecName: Full=10 kDa chaperonin;
AltName: Full=10 kDa antigen {ECO:0000303|PubMed:2902558};
AltName: Full=BCG-A heat shock protein {ECO:0000303|PubMed:2564178};
AltName: Full=GroES protein;
AltName: Full=Protein Cpn10;
Name=groS; Synonyms=cpn10, groES, mopB; OrderedLocusNames=Rv3418c;
ORFNames=MTCY78.11;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=2902558; DOI=10.1093/nar/16.18.9047;
Baird P.N., Hall L.M., Coates A.R.M.;
"A major antigen from Mycobacterium tuberculosis which is homologous
to the heat shock proteins groES from E. coli and the htpA gene
product of Coxiella burneti.";
Nucleic Acids Res. 16:9047-9047(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=2480990; DOI=10.1099/00221287-135-4-931;
Baird P.N., Hall L.M.C., Coates A.R.M.;
"Cloning and sequence analysis of the 10 kDa antigen gene of
Mycobacterium tuberculosis.";
J. Gen. Microbiol. 135:931-939(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=2564178; DOI=10.1093/nar/17.3.1254;
Shinnick T.M., Plikaytis B.P., Hyche A.D., van Landingham R.M.,
Walker L.L.;
"The Mycobacterium tuberculosis BCG-a protein has homology with the
Escherichia coli GroES protein.";
Nucleic Acids Res. 17:1254-1254(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=7681982; DOI=10.1073/pnas.90.7.2608;
Kong T.H., Coates A.R.M., Butcher P.D., Hickman C.J., Shinnick T.M.;
"Mycobacterium tuberculosis expresses two chaperonin-60 homologs.";
Proc. Natl. Acad. Sci. U.S.A. 90:2608-2612(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[6]
PROTEIN SEQUENCE OF 2-16.
PubMed=1371791;
Barnes P.F., Mehra V., Rivoire B., Fong S.J., Brennan P.J.,
Voegtline M.S., Minden P., Houghten R.A., Bloom B.R., Modlin R.L.;
"Immunoreactivity of a 10-kDa antigen of Mycobacterium tuberculosis.";
J. Immunol. 148:1835-1840(1992).
[7]
INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18227175; DOI=10.1128/IAI.01078-07;
Hu Y., Henderson B., Lund P.A., Tormay P., Ahmed M.T., Gurcha S.S.,
Besra G.S., Coates A.R.;
"A Mycobacterium tuberculosis mutant lacking the groEL homologue
cpn60.1 is viable but fails to induce an inflammatory response in
animal models of infection.";
Infect. Immun. 76:1535-1546(2008).
[8]
PUPYLATION AT LYS-100, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20066036; DOI=10.1371/journal.pone.0008589;
Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
Gygi S.P., Darwin K.H.;
"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium
tuberculosis.";
PLoS ONE 5:E8589-E8589(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[10]
INTERACTION WITH RIMI, ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR
METHIONINE.
PubMed=27353550; DOI=10.1038/srep28892;
Pathak D., Bhat A.H., Sapehia V., Rai J., Rao A.;
"Biochemical evidence for relaxed substrate specificity of Nalpha-
acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis.";
Sci. Rep. 6:28892-28892(2016).
[11]
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 2-100, AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
Taneja B., Mande S.C.;
"Three-dimensional structure of Mycobacterium tuberculosis chaperonin-
10 reveals a partially stable conformation for its mobile loop.";
Curr. Sci. 81:87-91(2001).
[12]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-100, AND SUBUNIT.
PubMed=12837792; DOI=10.1128/JB.185.14.4172-4185.2003;
Roberts M.M., Coker A.R., Fossati G., Mascagni P., Coates A.R.,
Wood S.P.;
"Mycobacterium tuberculosis chaperonin 10 heptamers self-associate
through their biologically active loops.";
J. Bacteriol. 185:4172-4185(2003).
[13]
STRUCTURE BY NMR OF 2-26.
Ciutti A., Spiga O., Giannozzi E., Scarselli M., Di Maro D.,
Calamandrei D., Niccolai N., Bernini A.;
"Solution Structure of 1-25 fragment of Cpn10 from Mycobacterium
tuberculosis.";
Submitted (MAY-2003) to the PDB data bank.
-!- FUNCTION: Binds to Cpn60 in the presence of Mg-ATP and suppresses
the ATPase activity of the latter.
-!- SUBUNIT: Heptamer of 7 subunits arranged in a domed ring (Ref.11,
PubMed:12837792). 2 rings join in their base to form a spherical
cage-like structure; both heptamers and tetradecamers exist in
solution (PubMed:12837792). Interacts with RimI (PubMed:27353550).
{ECO:0000269|PubMed:12837792, ECO:0000269|PubMed:27353550,
ECO:0000269|Ref.11}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- INDUCTION: Induced in response to heat shock (45 degrees Celsius),
pH 4, pH 10, ethanol, H(2)O(2), hyperosmolarity and starvation
(PubMed:18227175). {ECO:0000269|PubMed:18227175}.
-!- PTM: N-terminus is acetylated by RimI.
{ECO:0000269|PubMed:27353550}.
-!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
{ECO:0000269|PubMed:18227175}.
-!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X60350; CAA42908.1; -; Genomic_DNA.
EMBL; M25258; AAA25340.1; -; Genomic_DNA.
EMBL; X13739; CAA32003.1; -; Genomic_DNA.
EMBL; AL123456; CCP46240.1; -; Genomic_DNA.
PIR; S01381; BVMYBA.
RefSeq; NP_217935.1; NC_000962.3.
RefSeq; WP_003418028.1; NZ_KK339370.1.
PDB; 1HX5; X-ray; 3.50 A; A/B/C/D/E/F/G=2-100.
PDB; 1P3H; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-100.
PDB; 1P82; NMR; -; A=2-26.
PDB; 1P83; NMR; -; A=2-26.
PDBsum; 1HX5; -.
PDBsum; 1P3H; -.
PDBsum; 1P82; -.
PDBsum; 1P83; -.
ProteinModelPortal; P9WPE5; -.
SMR; P9WPE5; -.
STRING; 83332.Rv3418c; -.
iPTMnet; P9WPE5; -.
PaxDb; P9WPE5; -.
EnsemblBacteria; CCP46240; CCP46240; Rv3418c.
GeneID; 29702387; -.
GeneID; 887583; -.
KEGG; mtu:Rv3418c; -.
TubercuList; Rv3418c; -.
eggNOG; ENOG4105K5Y; Bacteria.
eggNOG; COG0234; LUCA.
KO; K04078; -.
OMA; PGRIDDN; -.
PhylomeDB; P9WPE5; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IDA:MTBBASE.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0035375; F:zymogen binding; IPI:CAFA.
GO; GO:0034605; P:cellular response to heat; IMP:MTBBASE.
GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
GO; GO:0040007; P:growth; IMP:MTBBASE.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MTBBASE.
GO; GO:0046677; P:response to antibiotic; IEP:MTBBASE.
GO; GO:0009408; P:response to heat; IEP:MTBBASE.
GO; GO:0006986; P:response to unfolded protein; IBA:GO_Central.
CDD; cd00320; cpn10; 1.
Gene3D; 2.30.33.40; -; 1.
HAMAP; MF_00580; CH10; 1.
InterPro; IPR020818; Chaperonin_GroES.
InterPro; IPR037124; Chaperonin_GroES_sf.
InterPro; IPR018369; Chaprnonin_Cpn10_CS.
InterPro; IPR011032; GroES-like_sf.
PANTHER; PTHR10772; PTHR10772; 1.
Pfam; PF00166; Cpn10; 1.
PRINTS; PR00297; CHAPERONIN10.
SMART; SM00883; Cpn10; 1.
SUPFAM; SSF50129; SSF50129; 1.
PROSITE; PS00681; CHAPERONINS_CPN10; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Reference proteome;
Stress response; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21969609,
ECO:0000269|PubMed:1371791,
ECO:0000269|PubMed:27353550}.
CHAIN 2 100 10 kDa chaperonin.
/FTId=PRO_0000174788.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:21969609,
ECO:0000269|PubMed:27353550}.
CROSSLNK 100 100 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-Cter in protein Pup).
{ECO:0000269|PubMed:20066036}.
STRAND 5 8 {ECO:0000244|PDB:1P3H}.
STRAND 12 17 {ECO:0000244|PDB:1P3H}.
STRAND 19 24 {ECO:0000244|PDB:1P83}.
TURN 25 27 {ECO:0000244|PDB:1HX5}.
STRAND 37 46 {ECO:0000244|PDB:1P3H}.
STRAND 53 56 {ECO:0000244|PDB:1P3H}.
STRAND 68 72 {ECO:0000244|PDB:1P3H}.
STRAND 77 81 {ECO:0000244|PDB:1P3H}.
STRAND 84 90 {ECO:0000244|PDB:1P3H}.
HELIX 91 93 {ECO:0000244|PDB:1P3H}.
STRAND 94 99 {ECO:0000244|PDB:1P3H}.
SEQUENCE 100 AA; 10804 MW; DE448187A56103FE CRC64;
MAKVNIKPLE DKILVQANEA ETTTASGLVI PDTAKEKPQE GTVVAVGPGR WDEDGEKRIP
LDVAEGDTVI YSKYGGTEIK YNGEEYLILS ARDVLAVVSK


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