PAFA2_RHOER
ID PAFA2_RHOER Reviewed; 447 AA.
AC P72270;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Pup--protein ligase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_02111};
DE AltName: Full=Pup-conjugating enzyme 2 {ECO:0000255|HAMAP-Rule:MF_02111};
GN Name=pafA2 {ECO:0000255|HAMAP-Rule:MF_02111}; ORFNames=ORF9(2);
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NI86/21;
RX PubMed=9254018; DOI=10.3109/10425179709034040;
RA Nagy I., Schoofs G., Vanderleyden J., De Mot R.;
RT "Further sequence analysis of the DNA regions with the Rhodococcus 20S
RT proteasome structural genes reveals extensive homology with Mycobacterium
RT leprae.";
RL DNA Seq. 7:225-228(1997).
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 involves the
CC side-chain carboxylate of the C-terminal glutamate of Pup and the side-
CC chain amino group of a substrate lysine. {ECO:0000255|HAMAP-
CC Rule:MF_02111}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + [prokaryotic ubiquitin-like protein]-L-glutamate +
CC [protein]-L-lysine = ADP + phosphate + N(6)-([prokaryotic ubiquitin-
CC like protein]-gamma-L-glutamyl)-[protein]-L-lysine.; EC=6.3.1.19;
CC Evidence={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. {ECO:0000255|HAMAP-
CC Rule:MF_02111}.
CC -!- MISCELLANEOUS: The reaction mechanism probably proceeds via the
CC activation of Pup by phosphorylation of its C-terminal glutamate, which
CC is then subject to nucleophilic attack by the substrate lysine,
CC resulting in an isopeptide bond and the release of phosphate as a good
CC leaving group. {ECO:0000255|HAMAP-Rule:MF_02111}.
CC -!- SIMILARITY: Belongs to the Pup ligase/Pup deamidase family. Pup-
CC conjugating enzyme subfamily. {ECO:0000255|HAMAP-Rule:MF_02111}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z82005; CAB04769.1; -; Genomic_DNA.
DR RefSeq; WP_020969669.1; NZ_WIDN01000105.1.
DR AlphaFoldDB; P72270; -.
DR SMR; P72270; -.
DR STRING; 1833.XU06_14785; -.
DR UniPathway; UPA00997; -.
DR UniPathway; UPA00998; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0070490; P:protein pupylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02111; Pup_ligase; 1.
DR InterPro; IPR022279; Pup_ligase.
DR InterPro; IPR004347; Pup_ligase/deamidase.
DR PANTHER; PTHR42307; PTHR42307; 1.
DR Pfam; PF03136; Pup_ligase; 1.
DR PIRSF; PIRSF018077; UCP018077; 1.
DR TIGRFAMs; TIGR03686; pupylate_PafA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Ubl conjugation pathway.
FT CHAIN 1..447
FT /note="Pup--protein ligase 2"
FT /id="PRO_0000395945"
FT ACT_SITE 52
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 4
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
SQ SEQUENCE 447 AA; 50346 MW; 053579DF4982C5D0 CRC64;
MGIETEFGVT CTFHGHRRLS PDEVARYLFR RVVSWGRSSN VFLRNGARLY LDVGSHPEYA
TAECDSLIQL VNHDRAGERV LEELLIDAEA RLAEEGIGGD IYLFKNNTDS AGNSYGCHEN
FLVARAGEFS RISDVLLPFL VTRQLICGAG KVLQTPKAAT FCLSQRAEHI WEGVSSATTR
SRPIINTRDE PHADAEKYRR LHVIVGDSNM AETTTMLKVG SAALVLEMIE AGVSFRDFAL
DNPIRAIREV SHDVTGKKPV RLAGGRQASA LDIQREYHAK AVEHLRNREP DPQVEQVVDL
WGRTLDAVEA QDFAKVDTEI DWVIKRKLFQ RYQDRHGFDL SDPKIAQLDL AYHDIKRGRG
VFDVLQRKGL VKRVTEDETI DDAVENPPQT TRAKLRGDFI TAAQAAGRDF TVDWVHLKLN
DQAQRTVLCK DPFRSVDERV ERLIASM
