(data stored in ACNUC7421 zone)

HOGENOM: STAHJ_1_PE1002

ID   STAHJ_1_PE1002                       STANDARD;      PRT;   539 AA.
AC   STAHJ_1_PE1002; Q4L7R4;
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; (STAHJ_1.PE1002).
GN   Name=groL; Synonyms=groEL; OrderedLocusNames=SH1002;
OS   STAPHYLOCOCCUS HAEMOLYTICUS JCSC1435.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAHJ_1.PE1002.
CC       Staphylococcus haemolyticus JCSC1435, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:CH60_STAHJ
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; Q4L7R4; -.
DR   EMBL; AP006716; BAE04311.1; -; Genomic_DNA.
DR   RefSeq; YP_252917.1; NC_007168.1.
DR   HSSP; Q9Z462; 1IOK.
DR   ProteinModelPortal; Q4L7R4; -.
DR   SMR; Q4L7R4; 2-523.
DR   STRING; Q4L7R4; -.
DR   EnsemblBacteria; EBSTAT00000045626; EBSTAP00000044077; EBSTAG00000045623.
DR   GeneID; 3482207; -.
DR   GenomeReviews; AP006716_GR; SH1002.
DR   KEGG; sha:SH1002; -.
DR   NMPDR; fig|279808.3.peg.1586; -.
DR   eggNOG; COG0459; -.
DR   GeneTree; EBGT00050000025062; -.
DR   OMA; ANPMGIR; -.
DR   ProtClustDB; PRK00013; -.
DR   BioCyc; SHAE279808:SH1002-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
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; STAHJ_1.PE1002; -.
KW   chaperonin GroEL;
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding.
SQ   SEQUENCE   539 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAKDLKFSED ARQAMLRGVD KLANAVKVTI GPKGRNVVLD KEYVAPLITN DGVTIAKEIE
     LEDPYENMGA KLVQEVANKT NEIAGDGTTT ATVLAQAMIQ EGLKNVTSGA NPVGLREGID
     KAVRVAVQAL HDISQKVENK NEIAQVGAIS AADEEIGKYI SEAMDKVGND GVITIEESNG
     LDTELEVVEG MQFDRGYQSP YMVTDSDKMI AELERPYILV TDKKISSFQD ILPLLEQVVQ
     SSRPILIVAD EVEGDALTNI VLNRMRGTFT AVAVKAPGFG DRRKAMLEDL AILTGATVIT
     DDLGLELKDA SIDMLGSANK VEVTKDNTTV VDGDGDDNSI DARVSQIKAQ IEETDSDFDR
     EKLQERLAKL AGGVAVIKVG AASETELKER KLRIEDALNS TRAAVEEGIV AGGGTALVNI
     YNKVDEIEAE GDVATGVNIV LKALSAPVRQ IAENAGLEGS VIVERLKHAD AGVGFNAATN
     EWVNMLEEGI VDPTKVTRSA LQHAASVAAM FLTTEAVVAT IPEPDNNDNP GMGGMPGMM
//

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