ARC_MYCTO
ID ARC_MYCTO Reviewed; 609 AA.
AC P9WQN4; L0T8W3; O33250; P63345; Q0G9Y7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Proteasome-associated ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
DE AltName: Full=AAA ATPase forming ring-shaped complexes {ECO:0000255|HAMAP-Rule:MF_02112};
DE Short=ARC {ECO:0000255|HAMAP-Rule:MF_02112};
DE AltName: Full=Mycobacterial proteasome ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
GN Name=mpa {ECO:0000255|HAMAP-Rule:MF_02112}; OrderedLocusNames=MT2175;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP BIOTECHNOLOGY, AND DISRUPTION PHENOTYPE.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=17041849; DOI=10.1086/508288;
RA Lamichhane G., Raghunand T.R., Morrison N.E., Woolwine S.C., Tyagi S.,
RA Kandavelou K., Bishai W.R.;
RT "Deletion of a Mycobacterium tuberculosis proteasomal ATPase homologue gene
RT produces a slow-growing strain that persists in host tissues.";
RL J. Infect. Dis. 194:1233-1240(2006).
CC -!- FUNCTION: ATPase which is responsible for recognizing, binding,
CC unfolding and translocation of pupylated proteins into the bacterial
CC 20S proteasome core particle. May be essential for opening the gate of
CC the 20S proteasome via an interaction with its C-terminus, thereby
CC allowing substrate entry and access to the site of proteolysis. Thus,
CC the C-termini of the proteasomal ATPase may function like a 'key in a
CC lock' to induce gate opening and therefore regulate proteolysis.
CC {ECO:0000255|HAMAP-Rule:MF_02112}.
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02112}.
CC -!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure that
CC caps the 20S proteasome core. Strongly interacts with the prokaryotic
CC ubiquitin-like protein Pup through a hydrophobic interface; the
CC interacting region of ARC lies in its N-terminal coiled-coil domain.
CC There is one Pup binding site per ARC hexamer ring. Upon ATP-binding,
CC the C-terminus of ARC interacts with the alpha-rings of the proteasome
CC core, possibly by binding to the intersubunit pockets.
CC {ECO:0000255|HAMAP-Rule:MF_02112}.
CC -!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil
CC domain that binds to protein Pup and functions as a docking station, an
CC interdomain involved in ARC hexamerization, and a C-terminal ATPase
CC domain of the AAA type. {ECO:0000255|HAMAP-Rule:MF_02112}.
CC -!- DISRUPTION PHENOTYPE: Mutants show a reduction in the in vivo growth
CC rate, but still persist in mouse lungs, and elicit reduced levels of
CC interferon-gamma production in the lungs. Expression of the genes lat
CC and MT3159 are highly up-regulated. {ECO:0000269|PubMed:17041849}.
CC -!- BIOTECHNOLOGY: When used as an immunizing agent, the mpa deletion
CC mutant provides significant protection against challenge with a
CC virulent strain of M.tuberculosis. It shows interesting properties as a
CC live attenuated vaccine for tuberculosis and could play a role in
CC generating a safe and effective M.tuberculosis-derived vaccine.
CC {ECO:0000269|PubMed:17041849}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_02112}.
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DR EMBL; AE000516; AAK46458.1; -; Genomic_DNA.
DR PIR; F70512; F70512.
DR RefSeq; WP_003411035.1; NZ_KK341227.1.
DR PDB; 3FP9; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=98-245.
DR PDBsum; 3FP9; -.
DR AlphaFoldDB; P9WQN4; -.
DR SMR; P9WQN4; -.
DR EnsemblBacteria; AAK46458; AAK46458; MT2175.
DR KEGG; mtc:MT2175; -.
DR PATRIC; fig|83331.31.peg.2345; -.
DR HOGENOM; CLU_036054_0_0_11; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0022623; C:proteasome-activating nucleotidase complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB.
DR Gene3D; 2.40.50.140; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02112; ARC_ATPase; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR InterPro; IPR041626; Prot_ATP_ID_OB_N.
DR InterPro; IPR022482; Proteasome_ATPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR Pfam; PF17758; Prot_ATP_OB_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03689; pup_AAA; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Coiled coil; Nucleotide-binding;
KW Proteasome; Virulence.
FT CHAIN 1..609
FT /note="Proteasome-associated ATPase"
FT /id="PRO_0000426745"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..609
FT /note="Docks into pockets in the proteasome alpha-ring"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT COILED 20..96
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT BINDING 296..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ SEQUENCE 609 AA; 67401 MW; 4D5F4E630614C58D CRC64;
MGESERSEAF GIPRDSPLSS GDAAELEQLR REAAVLREQL ENAVGSHAPT RSARDIHQLE
ARIDSLAARN SKLMETLKEA RQQLLALREE VDRLGQPPSG YGVLLATHDD DTVDVFTSGR
KMRLTCSPNI DAASLKKGQT VRLNEALTVV EAGTFEAVGE ISTLREILAD GHRALVVGHA
DEERVVWLAD PLIAEDLPDG LPEALNDDTR PRKLRPGDSL LVDTKAGYAF ERIPKAEVED
LVLEEVPDVS YADIGGLSRQ IEQIRDAVEL PFLHKELYRE YSLRPPKGVL LYGPPGCGKT
LIAKAVANSL AKKMAEVRGD DAHEAKSYFL NIKGPELLNK FVGETERHIR LIFQRAREKA
SEGTPVIVFF DEMDSIFRTR GTGVSSDVET TVVPQLLSEI DGVEGLENVI VIGASNREDM
IDPAILRPGR LDVKIKIERP DAEAAQDIYS KYLTEFLPVH ADDLAEFDGD RSACIKAMIE
KVVDRMYAEI DDNRFLEVTY ANGDKEVMYF KDFNSGAMIQ NVVDRAKKNA IKSVLETGQP
GLRIQHLLDS IVDEFAENED LPNTTNPDDW ARISGKKGER IVYIRTLVTG KSSSASRAID
TESNLGQYL