CH10_MYCTU
ID CH10_MYCTU Reviewed; 100 AA.
AC P9WPE5; L0TFJ8; P09621;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Co-chaperonin GroES {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=10 kDa antigen {ECO:0000303|PubMed:2902558};
DE AltName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=BCG-A heat shock protein {ECO:0000303|PubMed:2564178};
DE AltName: Full=Chaperonin-10 {ECO:0000255|HAMAP-Rule:MF_00580};
DE Short=Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580};
GN Name=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN Synonyms=cpn10, groS {ECO:0000255|HAMAP-Rule:MF_00580}, mopB;
GN OrderedLocusNames=Rv3418c; ORFNames=MTCY78.11;
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 [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=2902558; DOI=10.1093/nar/16.18.9047;
RA Baird P.N., Hall L.M., Coates A.R.M.;
RT "A major antigen from Mycobacterium tuberculosis which is homologous to the
RT heat shock proteins groES from E. coli and the htpA gene product of
RT Coxiella burneti.";
RL Nucleic Acids Res. 16:9047-9047(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=2480990; DOI=10.1099/00221287-135-4-931;
RA Baird P.N., Hall L.M.C., Coates A.R.M.;
RT "Cloning and sequence analysis of the 10 kDa antigen gene of Mycobacterium
RT tuberculosis.";
RL J. Gen. Microbiol. 135:931-939(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=2564178; DOI=10.1093/nar/17.3.1254;
RA Shinnick T.M., Plikaytis B.P., Hyche A.D., van Landingham R.M.,
RA Walker L.L.;
RT "The Mycobacterium tuberculosis BCG-a protein has homology with the
RT Escherichia coli GroES protein.";
RL Nucleic Acids Res. 17:1254-1254(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=7681982; DOI=10.1073/pnas.90.7.2608;
RA Kong T.H., Coates A.R.M., Butcher P.D., Hickman C.J., Shinnick T.M.;
RT "Mycobacterium tuberculosis expresses two chaperonin-60 homologs.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2608-2612(1993).
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-16.
RX PubMed=1371791;
RA Barnes P.F., Mehra V., Rivoire B., Fong S.J., Brennan P.J., Voegtline M.S.,
RA Minden P., Houghten R.A., Bloom B.R., Modlin R.L.;
RT "Immunoreactivity of a 10-kDa antigen of Mycobacterium tuberculosis.";
RL J. Immunol. 148:1835-1840(1992).
RN [7]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18227175; DOI=10.1128/iai.01078-07;
RA Hu Y., Henderson B., Lund P.A., Tormay P., Ahmed M.T., Gurcha S.S.,
RA Besra G.S., Coates A.R.;
RT "A Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is
RT viable but fails to induce an inflammatory response in animal models of
RT infection.";
RL Infect. Immun. 76:1535-1546(2008).
RN [8]
RP PUPYLATION AT LYS-100, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [10]
RP INTERACTION WITH RIMI, ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RX PubMed=27353550; DOI=10.1038/srep28892;
RA Pathak D., Bhat A.H., Sapehia V., Rai J., Rao A.;
RT "Biochemical evidence for relaxed substrate specificity of Nalpha-
RT acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis.";
RL Sci. Rep. 6:28892-28892(2016).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 2-100, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RA Taneja B., Mande S.C.;
RT "Three-dimensional structure of Mycobacterium tuberculosis chaperonin-10
RT reveals a partially stable conformation for its mobile loop.";
RL Curr. Sci. 81:87-91(2001).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-100, AND SUBUNIT.
RX PubMed=12837792; DOI=10.1128/jb.185.14.4172-4185.2003;
RA Roberts M.M., Coker A.R., Fossati G., Mascagni P., Coates A.R., Wood S.P.;
RT "Mycobacterium tuberculosis chaperonin 10 heptamers self-associate through
RT their biologically active loops.";
RL J. Bacteriol. 185:4172-4185(2003).
RN [13]
RP STRUCTURE BY NMR OF 2-26.
RA Ciutti A., Spiga O., Giannozzi E., Scarselli M., Di Maro D.,
RA Calamandrei D., Niccolai N., Bernini A.;
RT "Solution Structure of 1-25 fragment of Cpn10 from Mycobacterium
RT tuberculosis.";
RL Submitted (MAY-2003) to the PDB data bank.
CC -!- FUNCTION: Together with the chaperonin GroEL, plays an essential role
CC in assisting protein folding. The GroEL-GroES system forms a nano-cage
CC that allows encapsulation of the non-native substrate proteins and
CC provides a physical environment optimized to promote and accelerate
CC protein folding. GroES binds to the apical surface of the GroEL ring,
CC thereby capping the opening of the GroEL channel. {ECO:0000255|HAMAP-
CC Rule:MF_00580}.
CC -!- SUBUNIT: Heptamer of 7 subunits arranged in a domed ring (Ref.11,
CC PubMed:12837792). 2 rings join in their base to form a spherical cage-
CC like structure; both heptamers and tetradecamers exist in solution
CC (PubMed:12837792). Interacts with RimI (PubMed:27353550).
CC {ECO:0000269|PubMed:12837792, ECO:0000269|PubMed:27353550,
CC ECO:0000269|Ref.11}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}.
CC -!- INDUCTION: Induced in response to heat shock (45 degrees Celsius), pH
CC 4, pH 10, ethanol, H(2)O(2), hyperosmolarity and starvation
CC (PubMed:18227175). {ECO:0000269|PubMed:18227175}.
CC -!- PTM: N-terminus is acetylated by RimI. {ECO:0000269|PubMed:27353550}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:18227175}.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC Rule:MF_00580, ECO:0000305}.
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DR EMBL; X60350; CAA42908.1; -; Genomic_DNA.
DR EMBL; M25258; AAA25340.1; -; Genomic_DNA.
DR EMBL; X13739; CAA32003.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46240.1; -; Genomic_DNA.
DR PIR; S01381; BVMYBA.
DR RefSeq; NP_217935.1; NC_000962.3.
DR RefSeq; WP_003418028.1; NZ_NVQJ01000027.1.
DR PDB; 1HX5; X-ray; 3.50 A; A/B/C/D/E/F/G=2-100.
DR PDB; 1P3H; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-100.
DR PDB; 1P82; NMR; -; A=2-26.
DR PDB; 1P83; NMR; -; A=2-26.
DR PDBsum; 1HX5; -.
DR PDBsum; 1P3H; -.
DR PDBsum; 1P82; -.
DR PDBsum; 1P83; -.
DR AlphaFoldDB; P9WPE5; -.
DR SMR; P9WPE5; -.
DR STRING; 83332.Rv3418c; -.
DR iPTMnet; P9WPE5; -.
DR PaxDb; P9WPE5; -.
DR ABCD; P9WPE5; 1 sequenced antibody.
DR DNASU; 887583; -.
DR GeneID; 45427414; -.
DR GeneID; 66599586; -.
DR GeneID; 887583; -.
DR KEGG; mtu:Rv3418c; -.
DR TubercuList; Rv3418c; -.
DR eggNOG; COG0234; Bacteria.
DR OMA; EVKYSGE; -.
DR PhylomeDB; P9WPE5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IDA:MTBBASE.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0035375; F:zymogen binding; IPI:CAFA.
DR GO; GO:0034605; P:cellular response to heat; IMP:MTBBASE.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MTBBASE.
DR GO; GO:0046677; P:response to antibiotic; IEP:MTBBASE.
DR GO; GO:0009408; P:response to heat; IEP:MTBBASE.
DR CDD; cd00320; cpn10; 1.
DR Gene3D; 2.30.33.40; -; 1.
DR HAMAP; MF_00580; CH10; 1.
DR InterPro; IPR020818; Chaperonin_GroES.
DR InterPro; IPR037124; Chaperonin_GroES_sf.
DR InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR PANTHER; PTHR10772; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Reference proteome; Stress response; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1371791,
FT ECO:0000269|PubMed:27353550, ECO:0007744|PubMed:21969609"
FT CHAIN 2..100
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174788"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:27353550,
FT ECO:0007744|PubMed:21969609"
FT CROSSLNK 100
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1P3H"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:1P3H"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1P83"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1HX5"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1P3H"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1P3H"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1P3H"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1P3H"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1P3H"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1P3H"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1P3H"
SQ SEQUENCE 100 AA; 10804 MW; DE448187A56103FE CRC64;
MAKVNIKPLE DKILVQANEA ETTTASGLVI PDTAKEKPQE GTVVAVGPGR WDEDGEKRIP
LDVAEGDTVI YSKYGGTEIK YNGEEYLILS ARDVLAVVSK
