ID   PRS2_METTM              Reviewed;         372 AA.
AC   P42811; D9PXN2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Putative 26S proteasome regulatory subunit homolog MTBMA_c13930;
GN   OrderedLocusNames=MTBMA_c13930;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RA   Hungerer C., Weiss D., Thauer R.K., Jahn D.;
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
CC   -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
CC       degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC       complex confers ATP dependency and substrate specificity to the 26S
CC       complex (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADL58980.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X83691; CAA58665.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL58980.1; ALT_INIT; Genomic_DNA.
DR   PIR; S51137; S51137.
DR   AlphaFoldDB; P42811; -.
DR   SMR; P42811; -.
DR   STRING; 79929.MTBMA_c13930; -.
DR   EnsemblBacteria; ADL58980; ADL58980; MTBMA_c13930.
DR   KEGG; mmg:MTBMA_c13930; -.
DR   PATRIC; fig|79929.8.peg.1357; -.
DR   HOGENOM; CLU_000688_21_3_2; -.
DR   OMA; FGEWAPK; -.
DR   Proteomes; UP000000345; Chromosome.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Proteasome.
FT   CHAIN           1..372
FT                   /note="Putative 26S proteasome regulatory subunit homolog
FT                   MTBMA_c13930"
FT                   /id="PRO_0000084756"
FT   BINDING         164..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   372 AA;  42690 MW;  FCB5366A651B8E03 CRC64;
     MVKFNNIVYD PQLTDKKFPV KASDPEREAK LVVLQPVGYP FVCNLMESPR IDAVNKELFE
     IYARDQWEGF SATEGSYLFD QKLLPDYAFK IIRAHPDGSK ITRNTSIILL ENEREEFHEV
     KSDITMDDVI GQEDAKIKCR IIMRYLEDPD RFRDWAPRNV LFHGSPGTGK TMLAKSLANE
     LRVPLYLIKA TSLIGEHVGD GARQIHELYE LASKTAPSVI FIDEMDAIGL DRRFQSLRGD
     VSEVVNALLT EMDGINQNWG VVTIGATNNP ELLDNAIRSR FEEEIEFKLP GDDERRMMLE
     KYIETMPLDV DFSVDKLVKL TKGMSGRDIK ERVLKTALHR ALADESPRVE REHIEYALKE
     RDLKSEPRHM FA