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Pup--protein ligase (EC 6.3.1.19) (Proteasome accessory factor A) (Pup-conjugating enzyme)

 PAFA_GEOOG              Reviewed;         452 AA.
D2S6E4;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
02-MAR-2010, sequence version 1.
28-FEB-2018, entry version 48.
RecName: Full=Pup--protein ligase {ECO:0000255|HAMAP-Rule:MF_02111};
EC=6.3.1.19 {ECO:0000255|HAMAP-Rule:MF_02111};
AltName: Full=Proteasome accessory factor A {ECO:0000255|HAMAP-Rule:MF_02111};
AltName: Full=Pup-conjugating enzyme {ECO:0000255|HAMAP-Rule:MF_02111};
Name=pafA {ECO:0000255|HAMAP-Rule:MF_02111};
OrderedLocusNames=Gobs_2684;
Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 /
G-20).
Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
Geodermatophilus.
NCBI_TaxID=526225;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / G-20;
US DOE Joint Genome Institute (JGI-PGF);
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
Ivanova N., Munk A.C., Brettin T., Detter J.C., Han C., Larimer F.,
Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
"The complete genome of Geodermatophilus obscurus DSM 43160.";
Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the covalent attachment of the prokaryotic
ubiquitin-like protein modifier Pup to the proteasomal substrate
proteins, thereby targeting them for proteasomal degradation. This
tagging system is termed pupylation. The ligation reaction
involves the side-chain carboxylate of the C-terminal glutamate of
Pup and the side-chain amino group of a substrate lysine.
{ECO:0000255|HAMAP-Rule:MF_02111}.
-!- CATALYTIC ACTIVITY: ATP + [prokaryotic ubiquitin-like protein]-L-
glutamate + [protein]-L-lysine = ADP + phosphate + N(6)-
([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-
L-lysine. {ECO:0000255|HAMAP-Rule:MF_02111}.
-!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
{ECO:0000255|HAMAP-Rule:MF_02111}.
-!- PATHWAY: Protein modification; protein pupylation.
{ECO:0000255|HAMAP-Rule:MF_02111}.
-!- MISCELLANEOUS: The reaction mechanism probably proceeds via the
activation of Pup by phosphorylation of its C-terminal glutamate,
which is then subject to nucleophilic attack by the substrate
lysine, resulting in an isopeptide bond and the release of
phosphate as a good leaving group. {ECO:0000255|HAMAP-
Rule:MF_02111}.
-!- SIMILARITY: Belongs to the Pup ligase/Pup deamidase family. Pup-
conjugating enzyme subfamily. {ECO:0000255|HAMAP-Rule:MF_02111}.
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EMBL; CP001867; ADB75318.1; -; Genomic_DNA.
RefSeq; WP_012948751.1; NC_013757.1.
SMR; D2S6E4; -.
STRING; 526225.Gobs_2684; -.
MEROPS; U72.001; -.
PRIDE; D2S6E4; -.
EnsemblBacteria; ADB75318; ADB75318; Gobs_2684.
KEGG; gob:Gobs_2684; -.
eggNOG; ENOG4105DVV; Bacteria.
eggNOG; ENOG410XPTE; LUCA.
HOGENOM; HOG000264267; -.
KO; K13571; -.
OMA; CVSQRAE; -.
OrthoDB; POG091H0B56; -.
BioCyc; GOBS526225:G1GH8-2650-MONOMER; -.
UniPathway; UPA00997; -.
UniPathway; UPA00998; -.
Proteomes; UP000001382; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:InterPro.
GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
GO; GO:0070490; P:protein pupylation; IEA:UniProtKB-UniPathway.
HAMAP; MF_02111; Pup_ligase; 1.
InterPro; IPR022279; Pup_ligase.
InterPro; IPR004347; Pup_ligase/deamidase.
PANTHER; PTHR42307; PTHR42307; 1.
Pfam; PF03136; Pup_ligase; 1.
PIRSF; PIRSF018077; UCP018077; 1.
TIGRFAMs; TIGR03686; pupylate_PafA; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding;
Nucleotide-binding; Reference proteome; Ubl conjugation pathway.
CHAIN 1 452 Pup--protein ligase.
/FTId=PRO_0000395916.
ACT_SITE 57 57 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_02111}.
METAL 9 9 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_02111}.
METAL 55 55 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_02111}.
METAL 63 63 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_02111}.
BINDING 53 53 ATP. {ECO:0000255|HAMAP-Rule:MF_02111}.
BINDING 66 66 ATP; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_02111}.
BINDING 419 419 ATP. {ECO:0000255|HAMAP-Rule:MF_02111}.
SEQUENCE 452 AA; 51922 MW; 5E08F7BE431A9341 CRC64;
MERRIFGIET EYGVTCTFRG QRRLSPDEVA RYLFRRVVSW GRSSNVFLRN GSRLYLDVGS
HPEYATAECD DLSELVVHDK AGERILEGLL VDAEQRLAEE GVTGDIYLFK NNTDSAGNSY
GCHENYLVGR HGEFSRLADV LIPFLVSRQI VVGAGKVLQT PRGAIYCISQ RAEHIWEGVS
SATTRSRPII NTRDEPHADA ERYRRLHVIV GDSNMNETTT LLKVAVTDLV LRMIEAGVPI
RDMTLENPIR AIREISHDMT GRRKVRLANG KEMSALEIQS EYHSRAAEFV DREGFGPVHR
QMLELWGRVL KAVDTGDLSL IDREIDWATK YQLIERYRAK RDLPMSSPRI AQMDLAYHDI
SRTRGLYYLL ERNNQVDRVA HEPRVFEAKN VPPQTTRARL RGEFIRRAQE KRRDFTVDWV
HLKLNDQAQR TVLCKDPFKA VDERVDKLIA SM


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