CH601_ANASL
ID CH601_ANASL Reviewed; 543 AA.
AC Q9AMJ8;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=groL, groL1 {ECO:0000255|HAMAP-Rule:MF_00600};
OS Anabaena sp. (strain L31).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena;
OC unclassified Anabaena.
OX NCBI_TaxID=29412;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=18174150; DOI=10.1099/mic.0.2007/011064-0;
RA Rajaram H., Apte S.K.;
RT "Nitrogen status and heat-stress-dependent differential expression of the
RT cpn60 chaperonin gene influences thermotolerance in the cyanobacterium
RT Anabaena.";
RL Microbiology 154:317-325(2008).
RN [2]
RP PROTEIN SEQUENCE OF 42-70; 197-224 AND 454-468.
RA Rajaram H., Apte S.K.;
RL Submitted (DEC-2008) to UniProtKB.
RN [3]
RP INDUCTION.
RX PubMed=12728302; DOI=10.1007/s00203-003-0549-0;
RA Rajaram H., Apte S.K.;
RT "Heat-shock response and its contribution to thermotolerance of the
RT nitrogen-fixing cyanobacterium Anabaena sp. strain L-31.";
RL Arch. Microbiol. 179:423-429(2003).
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 heat shock under both nitrogen-fixing and nitrogen-
CC supplemented growth conditions. Induced within 5 to 15 minutes of the
CC start of heat stress, levels peak after 1 hour and expression continues
CC throughout the period of heat stress. {ECO:0000269|PubMed:12728302,
CC ECO:0000269|PubMed:18174150}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; AF324500; AAG49581.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AMJ8; -.
DR SMR; Q9AMJ8; -.
DR PRIDE; Q9AMJ8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
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 ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding; Stress response.
FT CHAIN 1..543
FT /note="Chaperonin GroEL 1"
FT /id="PRO_0000063263"
FT REGION 524..543
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 479..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 43
FT /note="Y -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 220..222
FT /note="AVD -> LLT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 57915 MW; E31EA260974BFD68 CRC64;
MAKRIIYNEN ARRALERGID ILAEAVAVTL GPKGRNVVLE KKYGAPQIVN DGVTIAKEIE
LEDHIENTGV ALIRQAASKT NDVAGDGTTT ATVLAHAIVK EGLRNVAAGA NAILLKRGID
KATNFLVDRI REHARSVEDS KAIAQVGAIS AGNDDEVRQM IAEALDKVGK EAVISLEEGK
SVTTELEVTE GMRFDKGYIS PYFATDPERM EAIFDEPFLA VDDKQIALVQ DLVPVLEPVA
RAGRPLVIIA EDIEKEALAT LVVNRLRGVL NVAAVKAPGF GDRRKAMLED IAILTGGQLI
TEDAGLKLDN TKLDSLGKAR RITITKDSTT IVAEGNDVAV KARVEQIRRQ MEETESSYDK
GKLQERLAKL SGGVAVVKVG AATETEMKDK KLRLEDAINA TKAAVEEGIV PGGGTTLAHL
TPELEAWANS TLKDEELTGA LIVARALPAP LKRIAENAGQ NGAVIAERVK EKEFNVDFNA
ATNEFVDMFS AGIVDPAKVT RSALQNALSY ACMVLTTGTV VDKPEPKDAA PAGVGGGGGD
FDY
