(data stored in ACNUC7421 zone)

SWISSPROT: PUP_RHOOB

ID   PUP_RHOOB               Reviewed;          64 AA.
AC   C1ASP8;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 43.
DE   RecName: Full=Prokaryotic ubiquitin-like protein Pup {ECO:0000255|HAMAP-Rule:MF_02106};
DE   AltName: Full=Bacterial ubiquitin-like modifier {ECO:0000255|HAMAP-Rule:MF_02106};
GN   Name=pup {ECO:0000255|HAMAP-Rule:MF_02106};
GN   OrderedLocusNames=ROP_05830;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein modifier that is covalently attached to lysine
CC       residues of substrate proteins, thereby targeting them for
CC       proteasomal degradation. The tagging system is termed pupylation.
CC       {ECO:0000255|HAMAP-Rule:MF_02106}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_02106}.
CC   -!- SUBUNIT: Strongly interacts with the proteasome-associated ATPase
CC       ARC through a hydrophobic interface; the interacting region of Pup
CC       lies in its C-terminal half. There is one Pup binding site per ARC
CC       hexamer ring. {ECO:0000255|HAMAP-Rule:MF_02106}.
CC   -!- DOMAIN: The N-terminal unstructured half of Pup provides a signal
CC       required to initiate unfolding and degradation by the proteasome
CC       but is not needed for pupylation, while the C-terminal helical
CC       half of Pup interacts with ARC to target proteins to the
CC       proteasome. {ECO:0000255|HAMAP-Rule:MF_02106}.
CC   -!- PTM: Is modified by deamidation of its C-terminal glutamine to
CC       glutamate by the deamidase Dop, a prerequisite to the subsequent
CC       pupylation process. {ECO:0000255|HAMAP-Rule:MF_02106}.
CC   -!- SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein
CC       family. {ECO:0000255|HAMAP-Rule:MF_02106}.
DR   EMBL; AP011115; BAH48830.1; -; Genomic_DNA.
DR   RefSeq; WP_005242990.1; NC_012522.1.
DR   SMR; C1ASP8; -.
DR   STRING; 632772.ROP_05830; -.
DR   EnsemblBacteria; BAH48830; BAH48830; ROP_05830.
DR   KEGG; rop:ROP_05830; -.
DR   PATRIC; fig|632772.20.peg.641; -.
DR   eggNOG; ENOG4105WFD; Bacteria.
DR   eggNOG; ENOG41123AH; LUCA.
DR   HOGENOM; HOG000245297; -.
DR   KO; K13570; -.
DR   OMA; AGQERME; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000002212; Chromosome.
DR   HAMAP; MF_02106; Pup; 1.
DR   InterPro; IPR008515; Ubiquitin-like_Pup.
DR   Pfam; PF05639; Pup; 1.
DR   TIGRFAMs; TIGR03687; pupylate_cterm; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ASP8.
DR   SWISS-2DPAGE; C1ASP8.
KW   Coiled coil; Complete proteome; Isopeptide bond;
KW   Ubl conjugation pathway.
FT   CHAIN         1     64       Prokaryotic ubiquitin-like protein Pup.
FT                                /FTId=PRO_0000390607.
FT   REGION       21     58       ARC ATPase binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_02106}.
FT   COILED       24     52       {ECO:0000255|HAMAP-Rule:MF_02106}.
FT   MOD_RES      64     64       Deamidated glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_02106}.
FT   CROSSLNK     64     64       Isoglutamyl lysine isopeptide (Gln-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins). {ECO:0000255|HAMAP-
FT                                Rule:MF_02106}.
SQ   SEQUENCE   64 AA;  6956 MW;  4A10C854A165702C CRC64;
     MAQEQTKRTG GGDEDDTPGG DGAAGQERRE KLAEDTDDLL DEIDDVLEEN AEDFVRAYVQ
     KGGQ
//

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