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60 kDa chaperonin 2 (65 kDa antigen) (Antigen A) (Cell wall protein A) (GroEL protein 2) (Heat shock protein 65) (Protein Cpn60-2)

 CH602_MYCTU             Reviewed;         540 AA.
P9WPE7; L0T3Q6; P06806; P0A520; Q48920; Q48931;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
07-NOV-2018, entry version 32.
RecName: Full=60 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00600};
AltName: Full=65 kDa antigen {ECO:0000303|PubMed:3029018};
AltName: Full=Antigen A;
AltName: Full=Cell wall protein A;
AltName: Full=GroEL protein 2 {ECO:0000255|HAMAP-Rule:MF_00600};
AltName: Full=Heat shock protein 65;
AltName: Full=Protein Cpn60-2 {ECO:0000255|HAMAP-Rule:MF_00600};
Name=groEL2;
Synonyms=groEL-2 {ECO:0000255|HAMAP-Rule:MF_00600}, groL2,
hsp65 {ECO:0000303|PubMed:7848059},
mtc28 {ECO:0000303|PubMed:21802426}; OrderedLocusNames=Rv0440;
ORFNames=MTV037.04;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=3029018; DOI=10.1128/jb.169.3.1080-1088.1987;
Shinnick T.M.;
"The 65-kilodalton antigen of Mycobacterium tuberculosis.";
J. Bacteriol. 169:1080-1088(1987).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-196.
STRAIN=12-14001;
Ros C., Belak K.;
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-183.
PubMed=7848059;
Kapur V., Li L.L., Hamrick M.R., Plikaytis B.B., Shinnick T.M.,
Telenti A., Jacobs W.R. Jr., Banerjee A., Cole S., Yuen K.Y.,
Clarridge J.E., Kreiswirth B.N., Musser J.M.;
"Rapid Mycobacterium species assignment and unambiguous identification
of mutations associated with antimicrobial resistance in Mycobacterium
tuberculosis by automated DNA sequencing.";
Arch. Pathol. Lab. Med. 119:131-138(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-178.
PubMed=7699930;
Hidaka E., Ueno I., Kawakami Y., Furuwatari C., Furihata K.,
Katsuyama T.;
"Detection and identification of mycobacteria by PCR-RFLP method.";
Rinsho Byori 43:155-161(1995).
[6]
FUNCTION AS A CHAPERONE, ATPASE ACTIVITY, AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15327959; DOI=10.1016/j.jmb.2004.07.066;
Qamra R., Srinivas V., Mande S.C.;
"Mycobacterium tuberculosis GroEL homologues unusually exist as lower
oligomers and retain the ability to suppress aggregation of substrate
proteins.";
J. Mol. Biol. 342:605-617(2004).
[7]
FUNCTION IN INFECTION.
PubMed=15809303; DOI=10.1074/jbc.M411379200;
Bulut Y., Michelsen K.S., Hayrapetian L., Naiki Y., Spallek R.,
Singh M., Arditi M.;
"Mycobacterium tuberculosis heat shock proteins use diverse Toll-like
receptor pathways to activate pro-inflammatory signals.";
J. Biol. Chem. 280:20961-20967(2005).
[8]
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).
[9]
PUPYLATION AT LYS-132, 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).
[10]
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).
[11]
INDUCTION.
PubMed=22464736; DOI=10.1016/j.tube.2012.03.001;
Stapleton M.R., Smith L.J., Hunt D.M., Buxton R.S., Green J.;
"Mycobacterium tuberculosis WhiB1 represses transcription of the
essential chaperonin GroEL2.";
Tuberculosis 92:328-332(2012).
[12]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 43-540, AND POSSIBLE SUBUNIT.
PubMed=15547284; DOI=10.1128/JB.186.23.8105-8113.2004;
Qamra R., Mande S.C.;
"Crystal structure of the 65-kilodalton heat shock protein, chaperonin
60.2, of Mycobacterium tuberculosis.";
J. Bacteriol. 186:8105-8113(2004).
[13]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), ATPASE ACTIVITY, AND SUBUNIT.
PubMed=21802426; DOI=10.1016/j.jmb.2011.07.026;
Shahar A., Melamed-Frank M., Kashi Y., Shimon L., Adir N.;
"The dimeric structure of the Cpn60.2 chaperonin of Mycobacterium
tuberculosis at 2.8 A reveals possible modes of function.";
J. Mol. Biol. 412:192-203(2011).
-!- FUNCTION: Prevents aggregation of substrate proteins and promotes
their refolding (PubMed:15327959). {ECO:0000269|PubMed:15327959}.
-!- FUNCTION: Recombinant extracellular protein activates expression
of NF-kappa-B in immortalized human dermal endothelial cells in a
TLR4-dependent, TLR2-independent manner. Activation occurs via
MYD88-dependent and -independent pathways and requires TIRAP,
TRIF, TRAM and MD-2 (some experiments done in mouse cells, mice do
not usually catch tuberculosis) (PubMed:15809303).
{ECO:0000269|PubMed:15809303}.
-!- SUBUNIT: Mostly homodimers in solution; does not seem to form
larger complexes (PubMed:21802426). {ECO:0000269|PubMed:15327959,
ECO:0000269|PubMed:21802426}.
-!- INTERACTION:
P9WI75:pknF; NbExp=3; IntAct=EBI-2945826, EBI-2945875;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
Secreted. Note=Extracellular protein is a potent stimulator of the
human immune system (PubMed:3029018).
{ECO:0000305|PubMed:3029018}.
-!- INDUCTION: Induced in response to heat shock (45 degrees Celsius),
pH 10, hyperosmolarity and starvation (PubMed:18227175). Repressed
by WhiB1, activated by Cmr (PubMed:22464736).
{ECO:0000269|PubMed:18227175, ECO:0000269|PubMed:22464736}.
-!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
{ECO:0000269|PubMed:18227175}.
-!- MISCELLANEOUS: Purified 65 kDa antigen can elicit a strong
delayed-type hypersensitivity reaction in experimental animals
infected with M.tuberculosis. This protein is one of the major
immunoreactive proteins of the mycobacteria (PubMed:3029018). It
contains epitopes that are common to various species of
mycobacteria (PubMed:7699930). {ECO:0000269|PubMed:3029018,
ECO:0000269|PubMed:7699930}.
-!- MISCELLANEOUS: The kcat for ATP is 0.18-0.28/min (PubMed:15327959,
PubMed:21802426). {ECO:0000269|PubMed:15327959,
ECO:0000269|PubMed:21802426}.
-!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
{ECO:0000255|HAMAP-Rule:MF_00600}.
-----------------------------------------------------------------------
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EMBL; M15467; AAA88232.1; -; Genomic_DNA.
EMBL; AL123456; CCP43171.1; -; Genomic_DNA.
EMBL; U55825; AAC44458.1; -; Genomic_DNA.
EMBL; U17957; AAB39076.1; -; Genomic_DNA.
EMBL; S76635; AAP31974.1; -; Genomic_DNA.
PIR; A26950; A26950.
RefSeq; NP_214954.1; NC_000962.3.
RefSeq; WP_003402236.1; NZ_NVQJ01000002.1.
PDB; 1SJP; X-ray; 3.20 A; A/B=43-540.
PDB; 3RTK; X-ray; 2.80 A; A/B=1-540.
PDBsum; 1SJP; -.
PDBsum; 3RTK; -.
ProteinModelPortal; P9WPE7; -.
SMR; P9WPE7; -.
IntAct; P9WPE7; 5.
STRING; 83332.Rv0440; -.
PaxDb; P9WPE7; -.
PRIDE; P9WPE7; -.
EnsemblBacteria; CCP43171; CCP43171; Rv0440.
GeneID; 886354; -.
KEGG; mtu:Rv0440; -.
TubercuList; Rv0440; -.
eggNOG; ENOG4105CJ9; Bacteria.
eggNOG; COG0459; LUCA.
KO; K04077; -.
OMA; TDTDKME; -.
PhylomeDB; P9WPE7; -.
PRO; PR:P9WPE7; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0042603; C:capsule; IDA:CAFA.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; HDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0006458; P:'de novo' protein folding; IBA:GO_Central.
GO; GO:0044406; P:adhesion of symbiont to host; IDA:MTBBASE.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:CAFA.
GO; GO:0042026; P:protein refolding; IDA:CAFA.
GO; GO:0009408; P:response to heat; IEP:MTBBASE.
GO; GO:0001666; P:response to hypoxia; IEP:MTBBASE.
CDD; cd03344; GroEL; 1.
Gene3D; 1.10.560.10; -; 1.
Gene3D; 3.30.260.10; -; 1.
Gene3D; 3.50.7.10; -; 1.
HAMAP; MF_00600; CH60; 1.
InterPro; IPR018370; Chaperonin_Cpn60_CS.
InterPro; IPR001844; Chaprnin_Cpn60.
InterPro; IPR002423; Cpn60/TCP-1.
InterPro; IPR027409; GroEL-like_apical_dom_sf.
InterPro; IPR027413; GROEL-like_equatorial_sf.
InterPro; IPR027410; TCP-1-like_intermed_sf.
Pfam; PF00118; Cpn60_TCP1; 1.
PRINTS; PR00298; CHAPERONIN60.
SUPFAM; SSF48592; SSF48592; 2.
SUPFAM; SSF52029; SSF52029; 1.
TIGRFAMs; TIGR02348; GroEL; 1.
PROSITE; PS00296; CHAPERONINS_CPN60; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
Isopeptide bond; Nucleotide-binding; Reference proteome; Secreted;
Ubl conjugation.
CHAIN 1 540 60 kDa chaperonin 2.
/FTId=PRO_0000063452.
CROSSLNK 132 132 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-Cter in protein Pup).
{ECO:0000269|PubMed:20066036}.
HELIX 64 77 {ECO:0000244|PDB:3RTK}.
HELIX 90 106 {ECO:0000244|PDB:3RTK}.
TURN 107 109 {ECO:0000244|PDB:3RTK}.
HELIX 112 132 {ECO:0000244|PDB:3RTK}.
HELIX 140 151 {ECO:0000244|PDB:3RTK}.
HELIX 154 166 {ECO:0000244|PDB:3RTK}.
STRAND 171 176 {ECO:0000244|PDB:3RTK}.
STRAND 179 182 {ECO:0000244|PDB:3RTK}.
STRAND 184 188 {ECO:0000244|PDB:3RTK}.
STRAND 190 194 {ECO:0000244|PDB:3RTK}.
STRAND 197 199 {ECO:0000244|PDB:3RTK}.
HELIX 200 202 {ECO:0000244|PDB:3RTK}.
TURN 206 209 {ECO:0000244|PDB:3RTK}.
STRAND 210 215 {ECO:0000244|PDB:3RTK}.
STRAND 217 225 {ECO:0000244|PDB:3RTK}.
TURN 229 231 {ECO:0000244|PDB:3RTK}.
HELIX 232 239 {ECO:0000244|PDB:3RTK}.
TURN 240 242 {ECO:0000244|PDB:3RTK}.
STRAND 245 252 {ECO:0000244|PDB:3RTK}.
HELIX 254 266 {ECO:0000244|PDB:3RTK}.
STRAND 271 275 {ECO:0000244|PDB:3RTK}.
HELIX 280 294 {ECO:0000244|PDB:3RTK}.
STRAND 298 300 {ECO:0000244|PDB:1SJP}.
STRAND 301 304 {ECO:0000244|PDB:3RTK}.
STRAND 307 309 {ECO:0000244|PDB:1SJP}.
TURN 312 314 {ECO:0000244|PDB:3RTK}.
STRAND 315 323 {ECO:0000244|PDB:3RTK}.
STRAND 328 333 {ECO:0000244|PDB:3RTK}.
HELIX 337 352 {ECO:0000244|PDB:3RTK}.
HELIX 357 372 {ECO:0000244|PDB:3RTK}.
STRAND 374 378 {ECO:0000244|PDB:3RTK}.
HELIX 386 407 {ECO:0000244|PDB:3RTK}.
STRAND 409 411 {ECO:0000244|PDB:3RTK}.
TURN 412 414 {ECO:0000244|PDB:3RTK}.
HELIX 415 418 {ECO:0000244|PDB:3RTK}.
HELIX 419 423 {ECO:0000244|PDB:3RTK}.
HELIX 433 443 {ECO:0000244|PDB:3RTK}.
HELIX 446 452 {ECO:0000244|PDB:3RTK}.
TURN 453 456 {ECO:0000244|PDB:3RTK}.
HELIX 459 468 {ECO:0000244|PDB:3RTK}.
STRAND 477 479 {ECO:0000244|PDB:3RTK}.
TURN 485 489 {ECO:0000244|PDB:3RTK}.
STRAND 491 493 {ECO:0000244|PDB:3RTK}.
HELIX 494 513 {ECO:0000244|PDB:3RTK}.
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


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