HSLV_BACAN
ID HSLV_BACAN Reviewed; 180 AA.
AC Q81WK5; Q6HUQ6; Q6KNY7;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=ATP-dependent protease subunit HslV {ECO:0000255|HAMAP-Rule:MF_00248};
DE EC=3.4.25.2 {ECO:0000255|HAMAP-Rule:MF_00248};
GN Name=hslV {ECO:0000255|HAMAP-Rule:MF_00248};
GN OrderedLocusNames=BA_3968, GBAA_3968, BAS3681;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protease subunit of a proteasome-like degradation complex
CC believed to be a general protein degrading machinery.
CC {ECO:0000255|HAMAP-Rule:MF_00248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent cleavage of peptide bonds with broad
CC specificity.; EC=3.4.25.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00248};
CC -!- ACTIVITY REGULATION: Allosterically activated by HslU binding.
CC {ECO:0000255|HAMAP-Rule:MF_00248}.
CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on each
CC side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV
CC complex is dependent on binding of ATP. {ECO:0000255|HAMAP-
CC Rule:MF_00248}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00248}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00248}.
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DR EMBL; AE016879; AAP27697.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33082.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT55983.1; -; Genomic_DNA.
DR RefSeq; NP_846211.1; NC_003997.3.
DR RefSeq; WP_000526272.1; NZ_WXXJ01000026.1.
DR RefSeq; YP_029932.1; NC_005945.1.
DR PDB; 3TY6; X-ray; 2.50 A; A/B/C/D/E/F=1-180.
DR PDBsum; 3TY6; -.
DR AlphaFoldDB; Q81WK5; -.
DR SMR; Q81WK5; -.
DR STRING; 260799.BAS3681; -.
DR MEROPS; T01.007; -.
DR DNASU; 1086806; -.
DR EnsemblBacteria; AAP27697; AAP27697; BA_3968.
DR EnsemblBacteria; AAT33082; AAT33082; GBAA_3968.
DR GeneID; 56653573; -.
DR GeneID; 67508464; -.
DR KEGG; ban:BA_3968; -.
DR KEGG; bar:GBAA_3968; -.
DR KEGG; bat:BAS3681; -.
DR PATRIC; fig|198094.11.peg.3938; -.
DR eggNOG; COG5405; Bacteria.
DR HOGENOM; CLU_093872_1_0_9; -.
DR OMA; IMKGNAR; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR CDD; cd01913; protease_HslV; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_00248; HslV; 1.
DR InterPro; IPR022281; ATP-dep_Prtase_HsIV_su.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR32194; PTHR32194; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PIRSF; PIRSF039093; HslV; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR03692; ATP_dep_HslV; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Cytoplasm; Hydrolase; Metal-binding;
KW Protease; Reference proteome; Sodium; Threonine protease.
FT CHAIN 1..180
FT /note="ATP-dependent protease subunit HslV"
FT /id="PRO_0000148077"
FT ACT_SITE 7
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT BINDING 165
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT BINDING 168
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT BINDING 171
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:3TY6"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:3TY6"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3TY6"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:3TY6"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3TY6"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3TY6"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3TY6"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3TY6"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:3TY6"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:3TY6"
FT TURN 93..97
FT /evidence="ECO:0007829|PDB:3TY6"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3TY6"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:3TY6"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:3TY6"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:3TY6"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3TY6"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:3TY6"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:3TY6"
SQ SEQUENCE 180 AA; 19449 MW; 31EF5206F2903A32 CRC64;
MGNFHATTIF AVHHNGECAM AGDGQVTMGN AVVMKHTARK VRKLFQGKVL AGFAGSVADA
FTLFEMFEGK LEEYNGNLQR AAVEMAKQWR GDKMLRQLEA MLIVMDKTTM LLVSGTGEVI
EPDDGILAIG SGGNYALSAG RALKQYASEH LTAKQIAKAS LEIAGDICVY TNHNIIVEEL
