PSA2_HALVD
ID PSA2_HALVD Reviewed; 249 AA.
AC Q9V2V5; D4GXU2;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Proteasome subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_00289};
DE AltName: Full=20S proteasome alpha subunit 2 {ECO:0000255|HAMAP-Rule:MF_00289};
DE AltName: Full=Proteasome core protein PsmA 2 {ECO:0000255|HAMAP-Rule:MF_00289};
GN Name=psmA2 {ECO:0000255|HAMAP-Rule:MF_00289}; Synonyms=psmC;
GN OrderedLocusNames=HVO_2923;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-31; 34-43 AND
RP 89-98, BLOCKAGE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=10482525; DOI=10.1128/jb.181.18.5814-5824.1999;
RA Wilson H.L., Aldrich H.C., Maupin-Furlow J.;
RT "Halophilic 20S proteasomes of the archaeon Haloferax volcanii:
RT purification, characterization, and gene sequence analysis.";
RL J. Bacteriol. 181:5814-5824(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP SUBUNIT, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12486053; DOI=10.1128/jb.185.1.165-174.2003;
RA Kaczowka S.J., Maupin-Furlow J.A.;
RT "Subunit topology of two 20S proteasomes from Haloferax volcanii.";
RL J. Bacteriol. 185:165-174(2003).
RN [4]
RP INDUCTION.
RX PubMed=15516591; DOI=10.1128/jb.186.22.7763-7772.2004;
RA Reuter C.J., Kaczowka S.J., Maupin-Furlow J.A.;
RT "Differential regulation of the PanA and PanB proteasome-activating
RT nucleotidase and 20S proteasomal proteins of the haloarchaeon Haloferax
RT volcanii.";
RL J. Bacteriol. 186:7763-7772(2004).
RN [5]
RP ACETYLATION AT MET-1.
RX PubMed=16950923; DOI=10.1128/jb.00943-06;
RA Humbard M.A., Stevens S.M. Jr., Maupin-Furlow J.A.;
RT "Posttranslational modification of the 20S proteasomal proteins of the
RT archaeon Haloferax volcanii.";
RL J. Bacteriol. 188:7521-7530(2006).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=18931121; DOI=10.1128/jb.01180-08;
RA Zhou G., Kowalczyk D., Humbard M.A., Rohatgi S., Maupin-Furlow J.A.;
RT "Proteasomal components required for cell growth and stress responses in
RT the haloarchaeon Haloferax volcanii.";
RL J. Bacteriol. 190:8096-8105(2008).
CC -!- FUNCTION: Component of the proteasome core, a large protease complex
CC with broad specificity involved in protein degradation. The H.volcanii
CC alpha1-beta-alpha2 proteasome is able to cleave oligopeptides after Tyr
CC and thus displays chymotrypsin-like activity. {ECO:0000255|HAMAP-
CC Rule:MF_00289, ECO:0000269|PubMed:10482525,
CC ECO:0000269|PubMed:12486053}.
CC -!- ACTIVITY REGULATION: The formation of the proteasomal ATPase PAN-20S
CC proteasome complex, via the docking of the C-termini of PAN into the
CC intersubunit pockets in the alpha-rings, triggers opening of the gate
CC for substrate entry. Interconversion between the open-gate and close-
CC gate conformations leads to a dynamic regulation of the 20S proteasome
CC proteolysis activity. {ECO:0000255|HAMAP-Rule:MF_00289}.
CC -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14 beta
CC subunits that assemble into four stacked heptameric rings, resulting in
CC a barrel-shaped structure. The two inner rings, each composed of seven
CC catalytic beta subunits, are sandwiched by two outer rings, each
CC composed of seven alpha subunits. H.volcanii produces at least 2 types
CC of 20S proteasomes: an alpha1-beta proteasome and a proteasome
CC containing all three subunits (alpha1, alpha2, and beta) that appears
CC to be asymmetrical with homo-oligomeric alpha1 and alpha2 rings
CC positioned on separate ends. The catalytic chamber with the active
CC sites is on the inside of the barrel. Has probably a gated structure,
CC the ends of the cylinder being occluded by the N-termini of the alpha-
CC subunits. Is likely capped at one or both ends by the proteasome
CC regulatory ATPase, PAN. {ECO:0000269|PubMed:10482525,
CC ECO:0000269|PubMed:12486053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
CC -!- INDUCTION: Up-regulated at mRNA and protein levels during transition
CC from exponential to stationary phase. {ECO:0000269|PubMed:15516591}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking psmA2 gene alone display
CC relatively normal growth rate and overall cell yield. However,
CC depletion of psmA1 and psmA2 together renders the cells inviable.
CC {ECO:0000269|PubMed:18931121}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|HAMAP-
CC Rule:MF_00289}.
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DR EMBL; AF126261; AAD53405.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE02793.1; -; Genomic_DNA.
DR PIR; T48679; T48679.
DR RefSeq; WP_004044756.1; NC_013967.1.
DR AlphaFoldDB; Q9V2V5; -.
DR SMR; Q9V2V5; -.
DR IntAct; Q9V2V5; 1.
DR STRING; 309800.C498_17805; -.
DR iPTMnet; Q9V2V5; -.
DR EnsemblBacteria; ADE02793; ADE02793; HVO_2923.
DR GeneID; 8926453; -.
DR KEGG; hvo:HVO_2923; -.
DR eggNOG; arCOG00971; Archaea.
DR HOGENOM; CLU_035750_4_1_2; -.
DR OMA; YQEQIPT; -.
DR OrthoDB; 57654at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_00289_A; Proteasome_A_A; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR019982; Proteasome_asu_arc.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Proteasome;
KW Reference proteome.
FT CHAIN 1..249
FT /note="Proteasome subunit alpha 2"
FT /id="PRO_0000124172"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:16950923"
SQ SEQUENCE 249 AA; 26727 MW; 7205A1A2B93E344E CRC64;
MNRNDKQAYD RGTSLFSPDG RIYQVEYARE AVKRGAPVLG VRTADGVVLA ALRSTPSELM
EAESIEKLHK LDDALGAATA GHVADARKLV DFARTTAQRE HLRYGEPIGV ETLTKTITDN
IQESTQSGGT RPYGASLLIG GVENGSGRLF ATDPSGTPQE WKAVAIGGHR EDVQAALEDG
YAEDLSLEDG LALAVEALVA ADEEIESDEL NLVTVSEAGY EIVDEETIAE LFADATADDE
SDETDEREE
