CH601_CHLPN
ID CH601_CHLPN Reviewed; 544 AA.
AC P31681; Q9JQ79;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Chaperonin GroEL 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL1 {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
GN OrderedLocusNames=CPn_0134, CP_0638, CpB0135;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=1682266; DOI=10.1128/iai.59.12.4665-4669.1991;
RA Kikuta L.C., Puolakkainen M., Kuo C.C., Campbell L.A.;
RT "Isolation and sequence analysis of the Chlamydia pneumoniae GroE operon.";
RL Infect. Immun. 59:4665-4669(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_00600}.
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 -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric
CC rings stacked back-to-back. Interacts with the co-chaperonin GroES.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- INDUCTION: By stress.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; M69217; AAA23126.1; -; Genomic_DNA.
DR EMBL; AE001363; AAD18287.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38453.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98344.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98068.1; -; Genomic_DNA.
DR PIR; B81556; B81556.
DR PIR; F86507; F86507.
DR PIR; S19023; S19023.
DR RefSeq; NP_224342.1; NC_000922.1.
DR RefSeq; WP_010882784.1; NZ_LN847257.1.
DR AlphaFoldDB; P31681; -.
DR SMR; P31681; -.
DR STRING; 115711.CP_0638; -.
DR MoonProt; P31681; -.
DR EnsemblBacteria; AAD18287; AAD18287; CPn_0134.
DR EnsemblBacteria; AAF38453; AAF38453; CP_0638.
DR GeneID; 45050179; -.
DR KEGG; cpa:CP_0638; -.
DR KEGG; cpj:groEL_1; -.
DR KEGG; cpn:CPn_0134; -.
DR KEGG; cpt:CpB0135; -.
DR PATRIC; fig|115713.3.peg.151; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_0; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020003; C:symbiont-containing vacuole; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:CAFA.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; IDA:CAFA.
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; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Stress response.
FT CHAIN 1..544
FT /note="Chaperonin GroEL 1"
FT /id="PRO_0000063328"
FT BINDING 30..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 87..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 481..483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 510
FT /note="A -> R (in Ref. 1; AAA23126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 58204 MW; 632BE406F5112C4F CRC64;
MAAKNIKYNE EARKKIHKGV KTLAEAVKVT LGPKGRHVVI DKSFGSPQVT KDGVTVAKEI
ELEDKHENMG AQMVKEVASK TADKAGDGTT TATVLAEAIY SEGLRNVTAG ANPMDLKRGI
DKAVKVVVDE LKKISKPVQH HKEIAQVATI SANNDSEIGN LIAEAMEKVG KNGSITVEEA
KGFETVLDVV EGMNFNRGYL SSYFSTNPET QECVLEDALI LIYDKKISGI KDFLPVLQQV
AESGRPLLII AEEIEGEALA TLVVNRLRAG FRVCAVKAPG FGDRRKAMLE DIAILTGGQL
VSEELGMKLE NTTLAMLGKA KKVIVTKEDT TIVEGLGNKP DIQARCDNIK KQIEDSTSDY
DKEKLQERLA KLSGGVAVIR VGAATEIEMK EKKDRVDDAQ HATIAAVEEG ILPGGGTALV
RCIPTLEAFL PMLANEDEAI GTRIILKALT APLKQIASNA GKEGAIICQQ VLARSANEGY
DALRDAYTDM IDAGILDPTK VTRSALESAA SIAGLLLTTE ALIADIPEEK SSSAPAMPSA
GMDY
