(data stored in ACNUC7421 zone)

SWISSPROT: PAFA_RHOOB

ID   PAFA_RHOOB              Reviewed;         452 AA.
AC   C1ASP4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=Pup--protein ligase {ECO:0000255|HAMAP-Rule:MF_02111};
DE            EC=6.3.1.19 {ECO:0000255|HAMAP-Rule:MF_02111};
DE   AltName: Full=Proteasome accessory factor A {ECO:0000255|HAMAP-Rule:MF_02111};
DE   AltName: Full=Pup-conjugating enzyme {ECO:0000255|HAMAP-Rule:MF_02111};
GN   Name=pafA {ECO:0000255|HAMAP-Rule:MF_02111};
GN   OrderedLocusNames=ROP_05790;
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: Catalyzes the covalent attachment of the prokaryotic
CC       ubiquitin-like protein modifier Pup to the proteasomal substrate
CC       proteins, thereby targeting them for proteasomal degradation. This
CC       tagging system is termed pupylation. The ligation reaction
CC       involves the side-chain carboxylate of the C-terminal glutamate of
CC       Pup and the side-chain amino group of a substrate lysine.
CC       {ECO:0000255|HAMAP-Rule:MF_02111}.
CC   -!- CATALYTIC ACTIVITY: ATP + [prokaryotic ubiquitin-like protein]-L-
CC       glutamate + [protein]-L-lysine = ADP + phosphate + N(6)-
CC       ([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-
CC       L-lysine. {ECO:0000255|HAMAP-Rule:MF_02111}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_02111}.
CC   -!- PATHWAY: Protein modification; protein pupylation.
CC       {ECO:0000255|HAMAP-Rule:MF_02111}.
CC   -!- MISCELLANEOUS: The reaction mechanism probably proceeds via the
CC       activation of Pup by phosphorylation of its C-terminal glutamate,
CC       which is then subject to nucleophilic attack by the substrate
CC       lysine, resulting in an isopeptide bond and the release of
CC       phosphate as a good leaving group. {ECO:0000255|HAMAP-
CC       Rule:MF_02111}.
CC   -!- SIMILARITY: Belongs to the Pup ligase/Pup deamidase family. Pup-
CC       conjugating enzyme subfamily. {ECO:0000255|HAMAP-Rule:MF_02111}.
DR   EMBL; AP011115; BAH48826.1; -; Genomic_DNA.
DR   SMR; C1ASP4; -.
DR   STRING; 632772.ROP_05790; -.
DR   EnsemblBacteria; BAH48826; BAH48826; ROP_05790.
DR   KEGG; rop:ROP_05790; -.
DR   PATRIC; fig|632772.20.peg.637; -.
DR   eggNOG; ENOG4105DVV; Bacteria.
DR   eggNOG; ENOG410XPTE; LUCA.
DR   HOGENOM; HOG000264267; -.
DR   KO; K13571; -.
DR   OMA; CVSQRAE; -.
DR   OrthoDB; POG091H0B56; -.
DR   UniPathway; UPA00997; -.
DR   UniPathway; UPA00998; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR   GO; GO:0070490; P:protein pupylation; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_02111; Pup_ligase; 1.
DR   InterPro; IPR022279; Pup_ligase.
DR   InterPro; IPR004347; Pup_ligase/deamidase.
DR   Pfam; PF03136; Pup_ligase; 1.
DR   PIRSF; PIRSF018077; UCP018077; 1.
DR   TIGRFAMs; TIGR03686; pupylate_PafA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ASP4.
DR   SWISS-2DPAGE; C1ASP4.
KW   ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Ubl conjugation pathway.
FT   CHAIN         1    452       Pup--protein ligase.
FT                                /FTId=PRO_0000395947.
FT   ACT_SITE     57     57       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_02111}.
FT   METAL         9      9       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_02111}.
FT   METAL        55     55       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_02111}.
FT   METAL        63     63       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_02111}.
FT   BINDING      53     53       ATP. {ECO:0000255|HAMAP-Rule:MF_02111}.
FT   BINDING      66     66       ATP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_02111}.
FT   BINDING     419    419       ATP. {ECO:0000255|HAMAP-Rule:MF_02111}.
SQ   SEQUENCE   452 AA;  51232 MW;  9AFB3E416C4C60D4 CRC64;
     MQRRIMGIET EFGVTCTFHG HRRLSPDEVA RYLFRRVVSW GRSSNVFLRN GARLYLDVGS
     HPEYATAECD NLIQLVNHDR AGERVLEELL IDAEQRLAEE GIGGDIYLFK NNTDSAGNSY
     GCHENFLVAR AGEFSRISDV LLPFLVTRQL ICGAGKVLQT PKAATFCLSQ RAEHIWEGVS
     SATTRSRPII NTRDEPHADA EKYRRLHVIV GDSNMSESTT MLKVGTAALV LEMIEAGVSF
     RDFALDNPIR AIREVSHDVT GRRPVRLAGG RQASALDIQR EYHARAVEHL QNRDPDPQVT
     QVVDLWGRML DAVETQDFAK VDTEIDWVIK RKLFQRYQDR HGFELADPKI AQLDLAYHDI
     KRGRGVFDVL QRKGLVKRIT EDETIEAAVD TPPQTTRAKL RGEFITAAQE AGRDFTVDWV
     HLKLNDQAQR TVLCKDPFRS VDERVERLIA SM
//

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