CH602_MYCTU
ID CH602_MYCTU Reviewed; 540 AA.
AC P9WPE7; L0T3Q6; P06806; P0A520; Q48920; Q48931;
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=Chaperonin GroEL 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=65 kDa antigen {ECO:0000303|PubMed:3029018};
DE AltName: Full=Antigen A;
DE AltName: Full=Cell wall protein A;
DE AltName: Full=Chaperonin-60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Heat shock protein 65 {ECO:0000303|PubMed:15809303};
DE Short=HSP65 {ECO:0000303|PubMed:15809303};
DE Contains:
DE RecName: Full=Cleaved form {ECO:0000305};
GN Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=cpn60.2 {ECO:0000303|PubMed:15327959},
GN groL2 {ECO:0000255|HAMAP-Rule:MF_00600},
GN hsp65 {ECO:0000303|PubMed:7848059}; OrderedLocusNames=Rv0440;
GN ORFNames=mtc28 {ECO:0000303|PubMed:21802426}, MTV037.04;
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 35801 / TMC 107 / Erdman;
RX PubMed=3029018; DOI=10.1128/jb.169.3.1080-1088.1987;
RA Shinnick T.M.;
RT "The 65-kilodalton antigen of Mycobacterium tuberculosis.";
RL J. Bacteriol. 169:1080-1088(1987).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-196.
RC STRAIN=12-14001;
RA Ros C., Belak K.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-183.
RX PubMed=7848059;
RA Kapur V., Li L.L., Hamrick M.R., Plikaytis B.B., Shinnick T.M., Telenti A.,
RA Jacobs W.R. Jr., Banerjee A., Cole S., Yuen K.Y., Clarridge J.E.,
RA Kreiswirth B.N., Musser J.M.;
RT "Rapid Mycobacterium species assignment and unambiguous identification of
RT mutations associated with antimicrobial resistance in Mycobacterium
RT tuberculosis by automated DNA sequencing.";
RL Arch. Pathol. Lab. Med. 119:131-138(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-178.
RX PubMed=7699930;
RA Hidaka E., Ueno I., Kawakami Y., Furuwatari C., Furihata K., Katsuyama T.;
RT "Detection and identification of mycobacteria by PCR-RFLP method.";
RL Rinsho Byori 43:155-161(1995).
RN [6]
RP FUNCTION AS A CHAPERONE, ATPASE ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15327959; DOI=10.1016/j.jmb.2004.07.066;
RA Qamra R., Srinivas V., Mande S.C.;
RT "Mycobacterium tuberculosis GroEL homologues unusually exist as lower
RT oligomers and retain the ability to suppress aggregation of substrate
RT proteins.";
RL J. Mol. Biol. 342:605-617(2004).
RN [7]
RP FUNCTION IN INFECTION.
RX PubMed=15809303; DOI=10.1074/jbc.m411379200;
RA Bulut Y., Michelsen K.S., Hayrapetian L., Naiki Y., Spallek R., Singh M.,
RA Arditi M.;
RT "Mycobacterium tuberculosis heat shock proteins use diverse Toll-like
RT receptor pathways to activate pro-inflammatory signals.";
RL J. Biol. Chem. 280:20961-20967(2005).
RN [8]
RP FUNCTION AS A CHAPERONE, 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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=19470749; DOI=10.1128/iai.00143-09;
RA Hickey T.B., Thorson L.M., Speert D.P., Daffe M., Stokes R.W.;
RT "Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial
RT surface, where Cpn60.2 facilitates efficient bacterial association with
RT macrophages.";
RL Infect. Immun. 77:3389-3401(2009).
RN [10]
RP PUPYLATION AT LYS-132, 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 [11]
RP FUNCTION IN VIRULENCE, SUBCELLULAR LOCATION, AND INTERACTION WITH CD43.
RX PubMed=20633027; DOI=10.1111/j.1462-5822.2010.01496.x;
RA Hickey T.B., Ziltener H.J., Speert D.P., Stokes R.W.;
RT "Mycobacterium tuberculosis employs Cpn60.2 as an adhesin that binds CD43
RT on the macrophage surface.";
RL Cell. Microbiol. 12:1634-1647(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
RP INDUCTION.
RX PubMed=22464736; DOI=10.1016/j.tube.2012.03.001;
RA Stapleton M.R., Smith L.J., Hunt D.M., Buxton R.S., Green J.;
RT "Mycobacterium tuberculosis WhiB1 represses transcription of the essential
RT chaperonin GroEL2.";
RL Tuberculosis 92:328-332(2012).
RN [14]
RP FUNCTION AS A CHAPERONE, ACTIVITY REGULATION, SUBUNIT, AND DOMAIN.
RX PubMed=22834700; DOI=10.1111/j.1365-2958.2012.08150.x;
RA Fan M., Rao T., Zacco E., Ahmed M.T., Shukla A., Ojha A., Freeke J.,
RA Robinson C.V., Benesch J.L., Lund P.A.;
RT "The unusual mycobacterial chaperonins: evidence for in vivo
RT oligomerization and specialization of function.";
RL Mol. Microbiol. 85:934-944(2012).
RN [15]
RP FUNCTION (CLEAVED FORM), SUBUNIT, SUBCELLULAR LOCATION, CLEAVAGE BY HIP1,
RP AND MUTAGENESIS OF 13-ARG-GLY-14.
RX PubMed=24830429; DOI=10.1371/journal.ppat.1004132;
RA Naffin-Olivos J.L., Georgieva M., Goldfarb N., Madan-Lala R., Dong L.,
RA Bizzell E., Valinetz E., Brandt G.S., Yu S., Shabashvili D.E., Ringe D.,
RA Dunn B.M., Petsko G.A., Rengarajan J.;
RT "Mycobacterium tuberculosis Hip1 modulates macrophage responses through
RT proteolysis of GroEL2.";
RL PLoS Pathog. 10:e1004132-e1004132(2014).
RN [16]
RP ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=26553853; DOI=10.1128/jb.00844-15;
RA Chilukoti N., Kumar C.M., Mande S.C.;
RT "GroEL2 of Mycobacterium tuberculosis reveals the importance of structural
RT pliability in chaperonin function.";
RL J. Bacteriol. 198:486-497(2016).
RN [17]
RP FUNCTION (CLEAVED FORM), INTERACTION WITH HOST HSPA9 (CLEAVED FORM), AND
RP SUBCELLULAR LOCATION (CLEAVED FORM).
RX PubMed=28288970; DOI=10.1242/bio.023119;
RA Joseph S., Yuen A., Singh V., Hmama Z.;
RT "Mycobacterium tuberculosis Cpn60.2 (GroEL2) blocks macrophage apoptosis
RT via interaction with mitochondrial mortalin.";
RL Biol. Open 6:481-488(2017).
RN [18]
RP FUNCTION IN VIRULENCE.
RX PubMed=29133346; DOI=10.1128/iai.00387-17;
RA Georgieva M., Sia J.K., Bizzell E., Madan-Lala R., Rengarajan J.;
RT "Mycobacterium tuberculosis GroEL2 modulates dendritic cell responses.";
RL Infect. Immun. 86:0-0(2018).
RN [19] {ECO:0007744|PDB:1SJP}
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 43-540, AND SUBUNIT.
RX PubMed=15547284; DOI=10.1128/jb.186.23.8105-8113.2004;
RA Qamra R., Mande S.C.;
RT "Crystal structure of the 65-kilodalton heat shock protein, chaperonin
RT 60.2, of Mycobacterium tuberculosis.";
RL J. Bacteriol. 186:8105-8113(2004).
RN [20] {ECO:0007744|PDB:3RTK}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), ATPASE ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=21802426; DOI=10.1016/j.jmb.2011.07.026;
RA Shahar A., Melamed-Frank M., Kashi Y., Shimon L., Adir N.;
RT "The dimeric structure of the Cpn60.2 chaperonin of Mycobacterium
RT tuberculosis at 2.8 A reveals possible modes of function.";
RL J. Mol. Biol. 412:192-203(2011).
CC -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential
CC role in assisting protein folding. The GroEL-GroES system forms a nano-
CC cage that allows encapsulation of the non-native substrate proteins and
CC provides a physical environment optimized to promote and accelerate
CC protein folding (By similarity). Prevents aggregation of substrate
CC proteins and promotes their refolding (PubMed:15327959,
CC PubMed:18227175, PubMed:22834700). In vitro, activity may be
CC independent of the presence or absence of the GroES co-chaperonin or
CC ATP (PubMed:15327959). Shows weak ATPase activity (PubMed:15327959,
CC PubMed:21802426). {ECO:0000255|HAMAP-Rule:MF_00600,
CC ECO:0000269|PubMed:15327959, ECO:0000269|PubMed:18227175,
CC ECO:0000269|PubMed:21802426, ECO:0000269|PubMed:22834700}.
CC -!- FUNCTION: Mediates association of bacteria with macrophages
CC (PubMed:19470749, PubMed:20633027). Acts as an adhesin that binds CD43
CC on the host macrophage surface (PubMed:20633027). The full-length
CC protein elicits robust pro-inflammatory responses from dendritic cells
CC (DCs) and promotes DC maturation and antigen presentation to T-cells.
CC DCs exposed to full-length GroEL2 induce strong antigen-specific gamma
CC interferon (IFN-gamma), interleukin-2 (IL-2), and IL-17A cytokine
CC responses from CD4(+) T-cells (PubMed:29133346). Recombinant
CC extracellular protein activates expression of NF-kappa-B in
CC immortalized human dermal endothelial cells in a TLR4-dependent, TLR2-
CC independent manner. Activation occurs via MYD88-dependent and
CC -independent pathways and requires TIRAP, TRIF, TRAM and MD-2 (some
CC experiments done in mouse cells, mice do not usually catch
CC tuberculosis) (PubMed:15809303). {ECO:0000269|PubMed:15809303,
CC ECO:0000269|PubMed:19470749, ECO:0000269|PubMed:20633027,
CC ECO:0000269|PubMed:29133346}.
CC -!- FUNCTION: [Cleaved form]: Cleaved, monomeric GroEL2 is biologically
CC relevant and significantly contributes to Hip1-mediated dampening of
CC macrophage responses during M.tuberculosis (Mtb) infection
CC (PubMed:24830429). Within macrophage, the cleaved form is able to
CC detach from the bacterial surface and crosses the phagosomal membrane
CC towards mitochondria organelles where it interacts with the host
CC stress-70 protein (HSPA9 or mortalin) and blocks macrophage apoptosis,
CC which promotes Mtb survival in the hostile macrophage environment
CC (PubMed:28288970). The cleaved form is poorly immunostimulatory and is
CC unable to promote DC maturation and antigen presentation. Proteolytic
CC cleavage of GroEL2 allows Mtb to prevent optimal DC-T-cell cross talk
CC during infection (PubMed:29133346). {ECO:0000269|PubMed:24830429,
CC ECO:0000269|PubMed:28288970, ECO:0000269|PubMed:29133346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00600};
CC -!- ACTIVITY REGULATION: Conditions that promote oligomer formation
CC increase the ATPase activity (PubMed:22834700). Chaperone activity is
CC fundamentally influenced by the interdomain communication, even if
CC oligomerization and the ability to recognize the substrates are
CC retained (PubMed:26553853). {ECO:0000269|PubMed:22834700,
CC ECO:0000269|PubMed:26553853}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat for ATPase activity is 0.28 min(-1) (PubMed:15327959). kcat
CC for ATPase activity is 0.18 min(-1) (PubMed:21802426).
CC {ECO:0000269|PubMed:15327959, ECO:0000269|PubMed:21802426};
CC -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric
CC rings stacked back-to-back (Probable). Also exists as lower oligomers,
CC including monomeric, dimeric, tetrameric and heptameric forms
CC (PubMed:15327959, PubMed:22834700, PubMed:15547284, PubMed:21802426,
CC PubMed:24830429). Forms monomers under standard conditions but
CC oligomerizes in the presence of high concentrations of ammonium salts
CC and either ATP or ADP (PubMed:22834700). Interacts with the co-
CC chaperonin GroES (By similarity). Interacts with the serine protease
CC Hip1 (PubMed:24830429). Interacts with host CD43 (PubMed:20633027).
CC {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:15327959,
CC ECO:0000269|PubMed:15547284, ECO:0000269|PubMed:20633027,
CC ECO:0000269|PubMed:21802426, ECO:0000269|PubMed:22834700,
CC ECO:0000269|PubMed:24830429, ECO:0000305|PubMed:22834700}.
CC -!- SUBUNIT: [Cleaved form]: Monomer (PubMed:24830429). Hip1-dependent
CC proteolytic cleavage converts multimeric GroEL2 to a monomeric form
CC (PubMed:24830429). Interacts with host mitochondrial mortalin
CC (PubMed:28288970). {ECO:0000269|PubMed:24830429,
CC ECO:0000269|PubMed:28288970}.
CC -!- INTERACTION:
CC P9WPE7; P9WI75: pknF; NbExp=3; IntAct=EBI-2945826, EBI-2945875;
CC -!- SUBCELLULAR LOCATION: Secreted, capsule {ECO:0000269|PubMed:19470749,
CC ECO:0000269|PubMed:20633027}. Cell surface
CC {ECO:0000269|PubMed:19470749, ECO:0000269|PubMed:20633027}. Secreted,
CC cell wall {ECO:0000269|PubMed:24830429}. Note=Although thought of as a
CC cytoplasmic chaperone this protein is routinely found extracellularly
CC in the absence of cell lysis. {ECO:0000305|PubMed:19470749}.
CC -!- SUBCELLULAR LOCATION: [Cleaved form]: Secreted
CC {ECO:0000269|PubMed:24830429}. Host mitochondrion
CC {ECO:0000269|PubMed:28288970}. Note=Exits phagosomal membrane and
CC reaches macrophage mitochondria. {ECO:0000269|PubMed:28288970}.
CC -!- INDUCTION: Induced in response to heat shock (45 degrees Celsius), pH
CC 10, hyperosmolarity and starvation (PubMed:18227175). Repressed by
CC WhiB1, activated by Cmr (PubMed:22464736).
CC {ECO:0000269|PubMed:18227175, ECO:0000269|PubMed:22464736}.
CC -!- DOMAIN: Each subunit is composed of an apical domain, an intermediate
CC domain and an equatorial domain (PubMed:26553853). The two hinges that
CC connect the equatorial and intermediate domains (EI hinge) and the
CC apical and intermediate domains (AI hinge) play a significant role in
CC the chaperonin activity (PubMed:26553853). The N-terminus is important
CC in determining the oligomerization status (PubMed:22834700).
CC {ECO:0000269|PubMed:22834700, ECO:0000269|PubMed:26553853}.
CC -!- PTM: Cleaved by the mycobacterial serine protease Hip1
CC (PubMed:24830429). Hip1-dependent cleavage of multimeric GroEL2 results
CC in release of cleaved monomeric GroEL2 into the extracellular milieu
CC (PubMed:24830429). {ECO:0000269|PubMed:24830429}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:18227175}.
CC -!- MISCELLANEOUS: M.tuberculosis contains two copies of the groEL gene,
CC groEL1 and groEL2. GroEL2 is probably the housekeeping chaperonin, with
CC the GroEL1 proteins having evolved, following an ancestral gene
CC duplication event, to take on a more specialized role or roles.
CC {ECO:0000305|PubMed:22834700}.
CC -!- MISCELLANEOUS: When coexpressed at high levels of expression with the
CC co-cheperonin GroES, can complement the E.coli groEL mutant.
CC {ECO:0000269|PubMed:18227175, ECO:0000269|PubMed:22834700}.
CC -!- MISCELLANEOUS: Purified 65 kDa antigen can elicit a strong delayed-type
CC hypersensitivity reaction in experimental animals infected with
CC M.tuberculosis. This protein is one of the major immunoreactive
CC proteins of the mycobacteria (PubMed:3029018). It contains epitopes
CC that are common to various species of mycobacteria (PubMed:7699930).
CC {ECO:0000269|PubMed:3029018, ECO:0000269|PubMed:7699930}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; M15467; AAA88232.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43171.1; -; Genomic_DNA.
DR EMBL; U55825; AAC44458.1; -; Genomic_DNA.
DR EMBL; U17957; AAB39076.1; -; Genomic_DNA.
DR EMBL; S76635; AAP31974.1; -; Genomic_DNA.
DR PIR; A26950; A26950.
DR RefSeq; NP_214954.1; NC_000962.3.
DR RefSeq; WP_003402236.1; NZ_NVQJ01000002.1.
DR PDB; 1SJP; X-ray; 3.20 A; A/B=43-540.
DR PDB; 3RTK; X-ray; 2.80 A; A/B=1-540.
DR PDBsum; 1SJP; -.
DR PDBsum; 3RTK; -.
DR AlphaFoldDB; P9WPE7; -.
DR SMR; P9WPE7; -.
DR IntAct; P9WPE7; 5.
DR STRING; 83332.Rv0440; -.
DR PaxDb; P9WPE7; -.
DR DNASU; 886354; -.
DR GeneID; 45424401; -.
DR GeneID; 886354; -.
DR KEGG; mtu:Rv0440; -.
DR TubercuList; Rv0440; -.
DR eggNOG; COG0459; Bacteria.
DR OMA; TDTDKME; -.
DR PhylomeDB; P9WPE7; -.
DR PRO; PR:P9WPE7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0042603; C:capsule; IDA:CAFA.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0044406; P:adhesion of symbiont to host; IDA:MTBBASE.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:CAFA.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IDA:CAFA.
DR GO; GO:0009408; P:response to heat; IEP:MTBBASE.
DR GO; GO:0001666; P:response to hypoxia; IEP:MTBBASE.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell wall; Chaperone; Host mitochondrion;
KW Isomerase; Isopeptide bond; Nucleotide-binding; Reference proteome;
KW Secreted; Ubl conjugation; Virulence.
FT CHAIN 1..540
FT /note="Chaperonin GroEL 2"
FT /id="PRO_0000063452"
FT CHAIN 14..540
FT /note="Cleaved form"
FT /evidence="ECO:0000305|PubMed:24830429"
FT /id="PRO_0000453198"
FT REGION 521..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 86..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT SITE 13..14
FT /note="Cleavage by Hip1"
FT /evidence="ECO:0000269|PubMed:24830429"
FT CROSSLNK 132
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT MUTAGEN 13..14
FT /note="RG->PP: Abolishes cleavage by Hip1."
FT /evidence="ECO:0000269|PubMed:24830429"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 90..106
FT /evidence="ECO:0007829|PDB:3RTK"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 112..132
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3RTK"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:3RTK"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:3RTK"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:1SJP"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1SJP"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 315..323
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 337..352
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 357..372
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 386..407
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:3RTK"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 419..423
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 433..443
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 446..452
FT /evidence="ECO:0007829|PDB:3RTK"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 459..468
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:3RTK"
FT TURN 485..489
FT /evidence="ECO:0007829|PDB:3RTK"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:3RTK"
FT HELIX 494..513
FT /evidence="ECO:0007829|PDB:3RTK"
SQ SEQUENCE 540 AA; 56727 MW; FF034616F709DA2A CRC64;
MAKTIAYDEE ARRGLERGLN ALADAVKVTL GPKGRNVVLE KKWGAPTITN DGVSIAKEIE
LEDPYEKIGA ELVKEVAKKT DDVAGDGTTT ATVLAQALVR EGLRNVAAGA NPLGLKRGIE
KAVEKVTETL LKGAKEVETK EQIAATAAIS AGDQSIGDLI AEAMDKVGNE GVITVEESNT
FGLQLELTEG MRFDKGYISG YFVTDPERQE AVLEDPYILL VSSKVSTVKD LLPLLEKVIG
AGKPLLIIAE DVEGEALSTL VVNKIRGTFK SVAVKAPGFG DRRKAMLQDM AILTGGQVIS
EEVGLTLENA DLSLLGKARK VVVTKDETTI VEGAGDTDAI AGRVAQIRQE IENSDSDYDR
EKLQERLAKL AGGVAVIKAG AATEVELKER KHRIEDAVRN AKAAVEEGIV AGGGVTLLQA
APTLDELKLE GDEATGANIV KVALEAPLKQ IAFNSGLEPG VVAEKVRNLP AGHGLNAQTG
VYEDLLAAGV ADPVKVTRSA LQNAASIAGL FLTTEAVVAD KPEKEKASVP GGGDMGGMDF
