CH602_ANASL
ID CH602_ANASL Reviewed; 557 AA.
AC Q7WVY0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=61 kDa chaperonin {ECO:0000303|PubMed:18174150};
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=Protein Cpn60 2 {ECO:0000250|UniProtKB:Q5SLM2, ECO:0000303|PubMed:18174150};
GN Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=cpn60 {ECO:0000312|EMBL:AAP94034.1},
GN groL2 {ECO:0000250|UniProtKB:Q5SLM2};
OS Anabaena sp. (strain L31).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena;
OC unclassified Anabaena.
OX NCBI_TaxID=29412;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP94034.1}
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 43-71; 196-209 AND 453-467.
RA Rajaram H., Apte S.K.;
RL Submitted (DEC-2008) to UniProtKB.
RN [3] {ECO:0000305}
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:0000250|UniProtKB:Q5SLM2,
CC ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- INDUCTION: By heat shock under nitrogen-fixing growth conditions.
CC Induced within 5 to 15 minutes of the start of heat stress, levels peak
CC after 1 hour and expression continues throughout the period of heat
CC stress. Repressed by heat stress under nitrogen-supplemented growth
CC conditions. {ECO:0000269|PubMed:12728302, 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; AY328922; AAP94034.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7WVY0; -.
DR SMR; Q7WVY0; -.
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; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding; Stress response.
FT CHAIN 1..557
FT /note="Chaperonin GroEL 2"
FT /id="PRO_0000364086"
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 478..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 557 AA; 58857 MW; 21251352C776211E CRC64;
MAKIISFDEE SRRALERGVN ALADAVKITL GPKGRNVLLE KKYGTPQIVN DGITVAKEIE
LEDPLENTGA RLIQEVASKT KDVAGDGTTT ATVLVQALIK EGLKNVAAGI NPVSLKRGID
KTTEALVEEI AKVAKPVEGS AIAQVATVSA GNDEEVGGMI AEAVERVTKD GVITVEESKS
LTTELDVVEG MHIDRGYISP YFITNNERQT VELENARILI TDKKINSIQE LVPVLKKVAR
LGQPLLIVAE DVEGDALATL VVNKARGVLS VAAIKAPGFG ERRKALLQDI AILTDGQLIS
EEIGLSLDTA SIDALCTART ITIDKENTTI VAGTTTKPEI QKRIGQIRKQ LEETDSEYDK
EKLQERIAKL AGGIAVIKVG AVPETELKDR KLRIENALNA TKAAVAESIG PGGGKTLIYL
ASKVDPIKAY FEEEEKIGAD IVKRALEAPL RQIADNAGEE GSVIVSRVKD SDFNVGYNAA
TGEFEDLIAA GIIDPAKVVR SALQNAASIA GLVLTTEAIV VEKPEKKPAV PADPGMGGMG
GMGGMGGMGG MGGMGMF
