⊟Summary[edit | edit source]
- pan ID?: SAUPAN003551000
- symbol?: hslV
- synonym: clpQ
- description?: ATP-dependent protease peptidase subunit
- ATP-dependent protease peptidase subunit
- HslU--HslV peptidase proteolytic subunit
- ATP-dependent protease subunit HslV
- ATP-dependent protease, subunit HslV
- ATP-dependent protease HslV
- ATP-dependent endopeptidase hsl proteolytic subunit
- ATP-dependent protease heat shock protein
- ATP-dependent protease HslVU, peptidase subunit
- putative ATP-dependent protease
- T01 family HslV component of HsIUV peptidase
descriptions from strain specific annotations:
- strand?: +
- coordinates?: 3887821..3888366
- synteny block?: BlockID0026280
- occurrence?: in 100% of 34 strains
hslV (clpQ) : hslUV proteolytic system threonine peptidase and proteolytic subunit HslV [1]
• A crystal structure is available : 6KR1
The HslUV proteolytic system is not as well substrate-characterized as other Clp proteases in staphylococci. In the presence of HslU and ATP, HslV is processed to generate a new N-terminus at with Thr-9 as the new catalytic N-terminal residue of a threonine peptidase. HslV oligomerizes as two rings of hexamers capped on either end by a ring of HslU hexamers. HslU then selectively unwinds substrate proteins and feeds them into the HslV proteolytic machine for degradation. The system is mildly induced under heat shock conditions but doesn't have a clear mutant phenotype.
⊟Orthologs[edit | edit source]
⊟Genome Viewer[edit | edit source]
COL | |
N315 | |
NCTC8325 | |
Newman | |
USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MSNTTLHATTIYAVRHNGKAAMAGDGQVTLGQQVIMKQTARKVRRLYEGKVLAGFAGSVA
N315 MSNTTLHATTIYAVRHNGKAAMAGDGQVTLGQQVIMKQTARKVRRLYEGKVLAGFAGSVA
NCTC8325 MSNTTLHATTIYAVRHNGKAAMAGDGQVTLGQQVIMKQTARKVRRLYEGKVLAGFAGSVA
Newman MSNTTLHATTIYAVRHNGKAAMAGDGQVTLGQQVIMKQTARKVRRLYEGKVLAGFAGSVA
USA300_FPR3757 MSNTTLHATTIYAVRHNGKAAMAGDGQVTLGQQVIMKQTARKVRRLYEGKVLAGFAGSVA
************************************************************
COL DAFTLFEKFETKLQQFSGNLERAAVELAQEWRGDKQLRQLEAMLIVMDKDAILVVSGTGE
N315 DAFTLFEKFETKLQQFSGNLERAAVELAQEWRGDKQLRQLEAMLIVMDKDAILVVSGTGE
NCTC8325 DAFTLFEKFETKLQQFSGNLERAAVELAQEWRGDKQLRQLEAMLIVMDKDAILVVSGTGE
Newman DAFTLFEKFETKLQQFSGNLERAAVELAQEWRGDKQLRQLEAMLIVMDKDAILVVSGTGE
USA300_FPR3757 DAFTLFEKFETKLQQFSGNLERAAVELAQEWRGDKQLRQLEAMLIVMDKDAILVVSGTGE
************************************************************
COL VIAPDDDLIAIGSGGNYALSAGRALKRHASHLSAEEMAYESLKVAADICVFTNDNIVVET
N315 VIAPDDDLIAIGSGGNYALSAGRALKRHASHLSAEEMAYESLKVAADICVFTNDNIVVET
NCTC8325 VIAPDDDLIAIGSGGNYALSAGRALKRHASHLSAEEMAYESLKVAADICVFTNDNIVVET
Newman VIAPDDDLIAIGSGGNYALSAGRALKRHASHLSAEEMAYESLKVAADICVFTNDNIVVET
USA300_FPR3757 VIAPDDDLIAIGSGGNYALSAGRALKRHASHLSAEEMAYESLKVAADICVFTNDNIVVET
************************************************************
COL L
N315 L
NCTC8325 L
Newman L
USA300_FPR3757 L
*
- ↑ Dorte Frees, Line E Thomsen, Hanne Ingmer
Staphylococcus aureus ClpYQ plays a minor role in stress survival.
Arch Microbiol: 2005, 183(4);286-91
[PubMed:15843987] [WorldCat.org] [DOI] (P p)Soyeon Jeong, Jinsook Ahn, Ae-Ran Kwon, Nam-Chul Ha
Cleavage-Dependent Activation of ATP-Dependent Protease HslUV from Staphylococcus aureus.
Mol Cells: 2020, 43(8);694-704
[PubMed:32694241] [WorldCat.org] [DOI] (I p)