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60 kDa chaperonin (57 kDa chlamydial hypersensitivity antigen) (GroEL protein) (Heat shock protein 60) (HSP60) (Protein Cpn60)

 CH60_CHLTR              Reviewed;         544 AA.
P0C0Z7; O84112; P17203;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 78.
RecName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
AltName: Full=57 kDa chlamydial hypersensitivity antigen;
AltName: Full=GroEL protein {ECO:0000255|HAMAP-Rule:MF_00600};
AltName: Full=Heat shock protein 60;
Short=HSP60;
AltName: Full=Protein Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
Name=groL {ECO:0000255|HAMAP-Rule:MF_00600};
Synonyms=groEL {ECO:0000255|HAMAP-Rule:MF_00600}, hypB, mopA;
OrderedLocusNames=CT_110;
Chlamydia trachomatis (strain D/UW-3/Cx).
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=272561;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=L2;
PubMed=1987066;
Cerrone M.C., Ma J.J., Stephens R.S.;
"Cloning and sequence of the gene for heat shock protein 60 from
Chlamydia trachomatis and immunological reactivity of the protein.";
Infect. Immun. 59:79-90(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=D/UW-3/Cx;
PubMed=9784136; DOI=10.1126/science.282.5389.754;
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V.,
Davis R.W.;
"Genome sequence of an obligate intracellular pathogen of humans:
Chlamydia trachomatis.";
Science 282:754-759(1998).
[3]
PROTEIN SEQUENCE OF 2-11.
Bini L., Santucci A., Magi B., Marzocchi B., Sanchez-Campillo M.,
Comanducci M., Christianen G., Birkelund S., Vtretou E., Ratti G.,
Pallini V.;
Submitted (SEP-1994) to UniProtKB.
-!- FUNCTION: Prevents misfolding and promotes the refolding and
proper assembly of unfolded polypeptides generated under stress
conditions (By similarity). This protein is implicated in the
pathogenesis of chlamydial disease. Inflammation elicited by the
57 kDa antigen may damage tissue, with progression to scarring of
conjunctival and fallopian tube mucosae, which respectively result
in blindness and infertility. {ECO:0000255|HAMAP-Rule:MF_00600}.
-!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of
7 subunits. {ECO:0000255|HAMAP-Rule:MF_00600}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: By stress.
-!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
{ECO:0000255|HAMAP-Rule:MF_00600}.
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EMBL; M58027; AAA23128.1; -; Genomic_DNA.
EMBL; AE001273; AAC67701.1; -; Genomic_DNA.
PIR; A71555; A71555.
PIR; B41479; B41479.
RefSeq; NP_219613.1; NC_000117.1.
RefSeq; WP_010725062.1; NC_000117.1.
PDB; 1ROJ; Model; -; B=-.
PDB; 1ROK; Model; -; B=-.
PDBsum; 1ROJ; -.
PDBsum; 1ROK; -.
ProteinModelPortal; P0C0Z7; -.
SMR; P0C0Z7; -.
PRIDE; P0C0Z7; -.
EnsemblBacteria; AAC67701; AAC67701; CT_110.
GeneID; 35550709; -.
GeneID; 884030; -.
KEGG; ctr:CT_110; -.
PATRIC; fig|272561.5.peg.120; -.
eggNOG; ENOG4105CJ9; Bacteria.
eggNOG; COG0459; LUCA.
InParanoid; P0C0Z7; -.
KO; K04077; -.
OMA; TDTDKME; -.
BioCyc; CTRA272561:G1G18-115-MONOMER; -.
Proteomes; UP000000431; Chromosome.
GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0044183; F:protein binding involved in protein folding; IBA:GO_Central.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0006458; P:'de novo' protein folding; IBA:GO_Central.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0042026; P:protein refolding; IEA:InterPro.
CDD; cd03344; GroEL; 1.
Gene3D; 1.10.560.10; -; 2.
Gene3D; 3.30.260.10; -; 2.
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.
SUPFAM; SSF54849; SSF54849; 1.
TIGRFAMs; TIGR02348; GroEL; 1.
PROSITE; PS00296; CHAPERONINS_CPN60; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; Nucleotide-binding; Reference proteome;
Stress response.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.3}.
CHAIN 2 544 60 kDa chaperonin.
/FTId=PRO_0000063332.
VARIANT 124 124 V -> A (in strain: L2).
VARIANT 131 131 I -> V (in strain: L2).
VARIANT 132 132 R -> K (in strain: L2).
VARIANT 189 189 I -> V (in strain: L2).
VARIANT 191 191 E -> D (in strain: L2).
VARIANT 217 217 D -> E (in strain: L2).
VARIANT 255 255 E -> V (in strain: L2).
VARIANT 264 264 V -> G (in strain: L2).
VARIANT 289 289 L -> F (in strain: L2).
CONFLICT 4 4 K -> D (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 544 AA; 58147 MW; 2CE404C5BBE6E623 CRC64;
MVAKNIKYNE EARKKIQKGV KTLAEAVKVT LGPKGRHVVI DKSFGSPQVT KDGVTVAKEV
ELADKHENMG AQMVKEVASK TADKAGDGTT TATVLAEAIY TEGLRNVTAG ANPMDLKRGI
DKAVKVVVDQ IRKISKPVQH HKEIAQVATI SANNDAEIGN LIAEAMEKVG KNGSITVEEA
KGFETVLDIV EGMNFNRGYL SSYFATNPET QECVLEDALV LIYDKKISGI KDFLPVLQQV
AESGRPLLII AEDIEGEALA TLVVNRIRGG FRVCAVKAPG FGDRRKAMLE DIAILTGGQL
ISEELGMKLE NANLAMLGKA KKVIVSKEDT TIVEGMGEKE ALEARCESIK KQIEDSSSDY
DKEKLQERLA KLSGGVAVIR VGAATEIEMK EKKDRVDDAQ HATIAAVEEG ILPGGGTALI
RCIPTLEAFL PMLTNEDEQI GARIVLKALS APLKQIAANA GKEGAIIFQQ VMSRSANEGY
DALRDAYTDM LEAGILDPAK VTRSALESAA SVAGLLLTTE ALIAEIPEEK PAAAPAMPGA
GMDY


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