(data stored in ACNUC30630 zone)

SWISSPROT: 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   11-DEC-2019, entry version 56.
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}.
DR   EMBL; CP001515; ACS46014.1; -; Genomic_DNA.
DR   RefSeq; WP_004218911.1; NC_012814.1.
DR   SMR; C6A7B6; -.
DR   EnsemblBacteria; ACS46014; ACS46014; Balac_0641.
DR   KEGG; blc:Balac_0641; -.
DR   PATRIC; fig|442563.4.peg.1227; -.
DR   HOGENOM; HOG000264267; -.
DR   KO; K13571; -.
DR   OMA; CVSQRAE; -.
DR   BioCyc; BANI580050:G1GV8-662-MONOMER; -.
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;
DR   PRODOM; C6A7B6.
DR   SWISS-2DPAGE; C6A7B6.
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   METAL           30
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT   METAL           75
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT   METAL           83
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT   BINDING         73
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT   BINDING         86
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02111"
FT   BINDING         450
FT                   /note="ATP"
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
//

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