(data stored in ACNUC7421 zone)

HOGENOM: CHLTJ_1_PE108

ID   CHLTJ_1_PE108                        STANDARD;      PRT;   544 AA.
AC   CHLTJ_1_PE108; C4PPB9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=60 kDa chaperonin;AltName: Full=GroEL protein;AltName:
DE   Full=Protein Cpn60; (CHLTJ_1.PE108).
GN   Name=hsp60_1; Synonyms=groEL, groL; OrderedLocusNames=JALI_1091;
OS   CHLAMYDIA TRACHOMATIS B/JALI20/OT.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=580049;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHLTJ_1.PE108.
CC       Chlamydia trachomatis B/Jali20/OT chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C4PPB9_CHLTJ
CC   -!- FUNCTION: Prevents misfolding and promotes the refolding and
CC       proper assembly of unfolded polypeptides generated under stress
CC       conditions (By similarity).
CC   -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of
CC       7 subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC   -!- GENE_FAMILY: HOG000076290 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C4PPB9; -.
DR   EMBL; FM872308; CAX10557.1; -; Genomic_DNA.
DR   RefSeq; YP_002887735.1; NC_012686.1.
DR   ProteinModelPortal; C4PPB9; -.
DR   SMR; C4PPB9; 3-527.
DR   STRING; C4PPB9; -.
DR   GeneID; 7881482; -.
DR   GenomeReviews; FM872308_GR; JALI_1091.
DR   KEGG; ctj:JALI_1091; -.
DR   OMA; MEDATIL; -.
DR   ProtClustDB; PRK00013; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:HAMAP.
DR   GO; GO:0042026; P:protein refolding; IEA:HAMAP.
DR   HAMAP; MF_00600; CH60; 1; -.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Chaprnin_Cpn60.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; GroEL-ATPase; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
DR   HOGENOMDNA; CHLTJ_1.PE108; -.
KW   chaperonin GroEL;
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding.
SQ   SEQUENCE   544 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVAKNIKYNE EARKKIQKGV KTLAEAVKVT LGPKGRHVVI DKSFGSPQVT KDGVTVAKEV
     ELADKHENMG AQMVKEVASK TADKAGDGTT TATVLAEAIY TEGLRNVTAG ANPMDLKRGI
     DKAVKVVVDQ IKKISKPVQH HKEIAQVATI SANNDAEIGN LIAEAMEKVG KNGSITVEEA
     KGFETVLDVV EGMNFNRGYL SSYFATNPET QECVLEDALV LIYDKKISGI KDFLPILQQV
     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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