| Tag | Content |
|---|
| CPLM ID | CPLM-009202 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 60 kDa chaperonin 1 |
Protein Synonyms/Alias | GroEL protein 1; Protein Cpn60 1 |
Gene Name | groL1 |
Gene Synonyms/Alias | groEL1; RPA1140 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 210 | YFVTNAEKMTVELDD | acetylation | [1] | | 445 | AGINIVLKALEAPIR | acetylation | [1] |
|
Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity). |
Sequence Annotation | |
Keyword | ATP-binding; Chaperone; Complete proteome; Cytoplasm; Nucleotide-binding. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 547 AA |
Protein Sequence | MAAKDVKFSG DARDRMLRGV DVLANAVKVT LGPKGRNVLI EKSFGAPRIT KDGVTVAKEV 60
ELEDKFENMG AQMVREVASK TNDLAGDGTT TATVLAQAIV REGAKAVAAG MNPMDLKRGI 120
EIAVAAVVKD IQKRAKPVAS SAEIAQVGTI SANGDAPIGK MIAQAMQKVG NEGVITVEEN 180
KSLETEVDIV EGMKFDRGYL SPYFVTNAEK MTVELDDAYI LLHEKKLSGL QSMLPVLEAV 240
VQSGKPLLII AEDVEGEALA TLVVNRLRGG LKVSAVKAPG FGDRRKAMLE DIAILTGGQL 300
ISEDLGIKLE TVTLKMLGRA KKVVIDKENT TIVNGAGKKP EIEARVSQIK AQIEETSSDY 360
DREKLQERLA KLAGGVAVIR VGGATEVEVK EKKDRVEDAL NATRAAVQEG IVPGGGVALL 420
RAKKAVGRIS NDNPDVQAGI NIVLKALEAP IRQIAENAGV EGSIVVGKIL ENKTETFGFD 480
AQTEEYVDML AKGIVDPAKV VRTALQDASS VASLLVTTEA MVAELPKADA PAMPAGGGMG 540
GMGGMGF 547 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |