CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009753
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Proteasome-associated ATPase 
Protein Synonyms/Alias
 AAA ATPase forming ring-shaped complexes; ARC; Mycobacterial proteasome ATPase 
Gene Name
 mpa 
Gene Synonyms/Alias
 Rv2115c; MT2175; MTCY261.11c 
Created Date
 July 27, 2013 
Organism
 Mycobacterium tuberculosis 
NCBI Taxa ID
 1773 
Lysine Modification
Position
Peptide
Type
References
591IRTLVTGKSSSASRApupylation[1]
Reference
 [1] Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis [corrected] .
 Festa RA, McAllister F, Pearce MJ, Mintseris J, Burns KE, Gygi SP, Darwin KH.
 PLoS One. 2010 Jan 6;5(1):e8589. [PMID: 20066036] 
Functional Description
 ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Is required but not sufficient to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types. 
Sequence Annotation
 NP_BIND 296 301 ATP (By similarity).
 REGION 608 609 Docks into pockets in the proteasome
 CROSSLNK 591 591 Isoglutamyl lysine isopeptide (Lys-Gln)  
Keyword
 3D-structure; ATP-binding; Chaperone; Coiled coil; Complete proteome; Isopeptide bond; Nucleotide-binding; Proteasome; Reference proteome; S-nitrosylation; Ubl conjugation; Virulence. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 609 AA 
Protein Sequence
MGESERSEAF GIPRDSPLSS GDAAELEQLR REAAVLREQL ENAVGSHAPT RSARDIHQLE 60
ARIDSLAARN SKLMETLKEA RQQLLALREE VDRLGQPPSG YGVLLATHDD DTVDVFTSGR 120
KMRLTCSPNI DAASLKKGQT VRLNEALTVV EAGTFEAVGE ISTLREILAD GHRALVVGHA 180
DEERVVWLAD PLIAEDLPDG LPEALNDDTR PRKLRPGDSL LVDTKAGYAF ERIPKAEVED 240
LVLEEVPDVS YADIGGLSRQ IEQIRDAVEL PFLHKELYRE YSLRPPKGVL LYGPPGCGKT 300
LIAKAVANSL AKKMAEVRGD DAHEAKSYFL NIKGPELLNK FVGETERHIR LIFQRAREKA 360
SEGTPVIVFF DEMDSIFRTR GTGVSSDVET TVVPQLLSEI DGVEGLENVI VIGASNREDM 420
IDPAILRPGR LDVKIKIERP DAEAAQDIYS KYLTEFLPVH ADDLAEFDGD RSACIKAMIE 480
KVVDRMYAEI DDNRFLEVTY ANGDKEVMYF KDFNSGAMIQ NVVDRAKKNA IKSVLETGQP 540
GLRIQHLLDS IVDEFAENED LPNTTNPDDW ARISGKKGER IVYIRTLVTG KSSSASRAID 600
TESNLGQYL 609 
Gene Ontology
 GO:0005618; C:cell wall; IDA:MTBBASE.
 GO:0005886; C:plasma membrane; IDA:MTBBASE.
 GO:0022623; C:proteasome-activating nucleotidase complex; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0016887; F:ATPase activity; IDA:UniProtKB.
 GO:0032182; F:small conjugating protein binding; IDA:UniProtKB.
 GO:0071732; P:cellular response to nitric oxide; IMP:UniProtKB.
 GO:0019941; P:modification-dependent protein catabolic process; IDA:UniProtKB.
 GO:0009405; P:pathogenesis; IMP:UniProtKB.
 GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:MTBBASE.
 GO:0051260; P:protein homooligomerization; IPI:MTBBASE.
 GO:0043335; P:protein unfolding; IDA:UniProtKB.
 GO:0051409; P:response to nitrosative stress; IMP:MTBBASE. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 IPR003960; ATPase_AAA_CS.
 IPR027417; P-loop_NTPase.
 IPR022482; Proteasome_ATPase. 
Pfam
 PF00004; AAA 
SMART
 SM00382; AAA 
PROSITE
 PS00674; AAA 
PRINTS