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CH60_PSEAE
ID   CH60_PSEAE              Reviewed;         547 AA.
AC   P30718;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 3.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
GN   OrderedLocusNames=PA4385;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1715325; DOI=10.1128/iai.59.9.3219-3226.1991;
RA   Sipos A., Klocke M., Frosch M.;
RT   "Cloning and sequencing of the genes coding for the 10- and 60-kDa heat
RT   shock proteins from Pseudomonas aeruginosa and mapping of a species-
RT   specific epitope.";
RL   Infect. Immun. 59:3219-3226(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P1118 / O:3;
RX   PubMed=7538307;
RA   Jensen P., Fomsgaard A., Hoiby N., Hindersson P.;
RT   "Cloning and nucleotide sequence comparison of the groE operon of
RT   Pseudomonas aeruginosa and Burkholderia cepacia.";
RL   APMIS 103:113-123(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PAO / AK957;
RX   PubMed=8857035; DOI=10.1139/m96-048;
RA   Farinha M.A., Mockett R., Went C.J., Jardine S., Naczynski L.M.,
RA   Kropinski A.M.;
RT   "Physical mapping of several heat-shock genes in Pseudomonas aeruginosa and
RT   the cloning of the mopA (GroEL) gene.";
RL   Can. J. Microbiol. 42:326-334(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-11.
RC   STRAIN=BN-1;
RA   Noman M., Qader U.L., Aman A., Bano S., Azhar A., Basit A.;
RL   Submitted (AUG-2009) to UniProtKB.
RN   [6]
RP   PROTEIN SEQUENCE OF 16-28; 64-75; 81-105; 143-168; 172-197; 232-268;
RP   323-345 AND 405-498.
RC   STRAIN=ATCC 33467 / type 1 smooth, and ATCC 33468 / type 2 mucoid;
RA   Liddor M.;
RT   "Biofouling in water treatment systems: effect of membrane properties on
RT   biofilm formation.";
RL   Thesis (2005), Ben-Gurion University, Israel.
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   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR   EMBL; M63957; AAA25830.1; -; Genomic_DNA.
DR   EMBL; S77424; AAB34346.1; -; Genomic_DNA.
DR   EMBL; U17072; AAA53369.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG07773.1; -; Genomic_DNA.
DR   PIR; B43606; B43606.
DR   PIR; B83098; B83098.
DR   RefSeq; NP_253075.1; NC_002516.2.
DR   RefSeq; WP_003094059.1; NZ_QZGE01000004.1.
DR   AlphaFoldDB; P30718; -.
DR   SMR; P30718; -.
DR   STRING; 287.DR97_1563; -.
DR   PaxDb; P30718; -.
DR   PRIDE; P30718; -.
DR   EnsemblBacteria; AAG07773; AAG07773; PA4385.
DR   GeneID; 881348; -.
DR   KEGG; pae:PA4385; -.
DR   PATRIC; fig|208964.12.peg.4593; -.
DR   PseudoCAP; PA4385; -.
DR   HOGENOM; CLU_016503_3_0_6; -.
DR   InParanoid; P30718; -.
DR   OMA; TDTDKME; -.
DR   PhylomeDB; P30718; -.
DR   BioCyc; PAER208964:G1FZ6-4471-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW   Nucleotide-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.5"
FT   CHAIN           2..547
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063486"
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         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        80..82
FT                   /note="KAN -> RPT (in Ref. 1; AAA25830 and 2; AAB34346)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="A -> P (in Ref. 1; AAA25830)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138..139
FT                   /note="CA -> WR (in Ref. 1; AAA25830)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319..320
FT                   /note="NA -> KP (in Ref. 1; AAA25830)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370
FT                   /note="A -> G (in Ref. 3; AAA53369)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="R -> P (in Ref. 1; AAA25830 and 2; AAB34346)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        451
FT                   /note="L -> V (in Ref. 1; AAA25830 and 2; AAB34346)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   547 AA;  57086 MW;  FB82EB49D0F4748D CRC64;
     MAAKEVKFGD SARKKMLVGV NVLADAVKAT LGPKGRNVVL DKSFGAPTIT KDGVSVAKEI
     ELKDKFENMG AQLVKDVASK ANDAAGDGTT TATVLAQAIV NEGLKAVAAG MNPMDLKRGI
     DKATVAIVAQ LKELAKPCAD TKAIAQVGTI SANSDESIGQ IIAEAMEKVG KEGVITVEEG
     SGLENELSVV EGMQFDRGYL SPYFVNKPDT MAAELDSPLL LLVDKKISNI REMLPVLEAV
     AKAGRPLLIV AEDVEGEALA TLVVNNMRGI VKVAAVKAPG FGDRRKAMLQ DIAILTGGTV
     ISEEVGLSLE GATLEHLGNA KRVVINKENT TIIDGAGVQA DIEARVLQIR KQIEETTSDY
     DREKLQERLA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVPGGGVALV
     RALQAIEGLK GDNEEQNVGI ALLRRAVESP LRQIVANAGD EPSVVVDKVK QGSGNYGFNA
     ATGVYGDMIE MGILDPAKVT RSALQAAASI GGLMITTEAM VAEIVEDKPA MGGMPDMGGM
     GGMGGMM
 
 
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