PAFA_BIFLB
ID PAFA_BIFLB Reviewed; 496 AA.
AC C6A7B6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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}; OrderedLocusNames=Balac_0641;
OS Bifidobacterium animalis subsp. lactis (strain Bl-04 / DGCC2908 / RB 4825 /
OS SD5219).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=580050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bl-04 / DGCC2908 / RB 4825 / SD5219;
RX PubMed=19376856; DOI=10.1128/jb.00155-09;
RA Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., Richards M.,
RA Horvath P., Coute-Monvoisin A.-C., Leyer G., Rendulic S., Steele J.L.,
RA Broadbent J.R., Oberg T., Dudley E.G., Schuster S., Romero D.A.,
RA Roberts R.F.;
RT "Comparison of the complete genome sequences of Bifidobacterium animalis
RT subsp. lactis DSM 10140 and Bl-04.";
RL J. Bacteriol. 191:4144-4151(2009).
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}.
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DR EMBL; CP001515; ACS46014.1; -; Genomic_DNA.
DR RefSeq; WP_004218911.1; NC_012814.1.
DR AlphaFoldDB; C6A7B6; -.
DR SMR; C6A7B6; -.
DR GeneID; 66532994; -.
DR KEGG; blc:Balac_0641; -.
DR PATRIC; fig|442563.4.peg.1227; -.
DR HOGENOM; CLU_040524_0_1_11; -.
DR OMA; CVSQRAE; -.
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.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Ubl conjugation pathway.
FT CHAIN 1..496
FT /note="Pup--protein ligase"
FT /id="PRO_0000395897"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT BINDING 450
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
SQ SEQUENCE 496 AA; 55439 MW; 24574FD9C873927A CRC64;
MPQLHDSGSR AIQPSDQTHQ HDFARIFGIE TEYGVSVTDI PEPMDASHVA MTMFQPVVRR
ARSTNTYVEN GSRLYLDVGS HPEYATAEAI CPSDALLSDL AGEQTMRSMG LDAQRRLRES
DAQNRHATLH LYKNNADSAG HSFGCHENYL VRRFVNLDMI QHVLLPFLIT RQIYTGAGRF
DGERLLFTQR AAFVDETVSS ATTRSRPMIN TRDEPHANPD DYRRLHVIIG DSNRSQWATL
MKCATTHLVL CMMEHAARSG CETELEAFAL ADPIAANHAI NTDGAHARIA LAAGRSTTAL
ELQQMMLEQV ESFAAHHGDA LEASLRYDAL CNVEWIVGQW RWVLDRLAAN DIETLSHVVD
WASKQVFFNR LQSRGTVTPA RLRQLDLDYH DIANGRLYPS LCAHGLMRTL VDADQIHDAV
STPPPHTRAV LRGRFVAAAS HTDAVYDCDW TTLKLVRPVH MEAVLLDPFH DEPTKQYDKL
MGELGDARAD GDEAPV
