ID F0IJK5_STRSA Unreviewed; 809 AA.
AC F0IJK5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:EGD37276.1};
GN Name=clpC {ECO:0000313|EMBL:EGD37276.1};
GN ORFNames=HMPREF9383_0307 {ECO:0000313|EMBL:EGD37276.1};
OS Streptococcus sanguinis SK150.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888811 {ECO:0000313|EMBL:EGD37276.1, ECO:0000313|Proteomes:UP000003530};
RN [1] {ECO:0000313|EMBL:EGD37276.1, ECO:0000313|Proteomes:UP000003530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK150 {ECO:0000313|EMBL:EGD37276.1,
RC ECO:0000313|Proteomes:UP000003530};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGD37276.1}.
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DR EMBL; AEXY01000004; EGD37276.1; -; Genomic_DNA.
DR RefSeq; WP_002908546.1; NZ_GL872442.1.
DR AlphaFoldDB; F0IJK5; -.
DR PATRIC; fig|888811.3.peg.299; -.
DR HOGENOM; CLU_005070_4_1_9; -.
DR Proteomes; UP000003530; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000313|EMBL:EGD37276.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EGD37276.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 809 AA; 89734 MW; E4F8A0F6DAB1E31F CRC64;
MKYSKALIES LEAAQLLAGH FTTDYLESWH LLIALANNPY SVAGSVLNEF PVEVDGFEEA
AFQITGQAYQ KDGHFELLPF SYRLEELFEE AGQIAEAVRA KHVGTEHVLL AMLFDRGTLA
SRILEFTGFS YEDKEQGPKI SDLRKVLEQR AGWGKEDIKA IRSLNKGVMA AKQTMANMMG
MPASTSGGLE DYTRDLTELA RDGRLEPVIG RDQEISRIVQ ILSRKTKNNP VLVGDAGVGK
TALALGLAQR VAAGQVPAEL AKMRVLELDL MNVVAGTRFR GDFEERMNNI INDIEEDGHV
ILFIDELHTI MGSGSGIDST LDAANILKPA LARGTLRTVG ATTQEEYQKH IEKDAALSRR
FAKVSIEEPN MADSIVILQG LRKSYEDHHK VQISDQAIET AVKYAHRYLT SKHLPDSAID
LLDEASATVQ NRGPQNYEQS DLTPVDQALM AADFKKVSQL LEQEQQPKLY KLKVEEDDVL
ATLSGLSGIP VQKLTQTDAK KYLNLETELH KRVIGQDEAI SAISRAIRRN QSGIRSSKRP
IGSFMFLGPT GVGKTELAKA LAESLFDDES ALIRFDMSEY MEKFAASRLN GAPPGYVGYE
EGGELTEKVR NRPYSVLLFD EVEKAHPDIF NVLLQVLDDG QLTDSKGRKV DFSNTIIIMT
SNLGATSLRD DKTVGFGARD IRLDHANMEK RMLEELKKAY RPEFINRIDE KVVFHSLSAE
DMQEVVKVMV KPLIASLTEK GIELKFQASA LKLLAQEGYD VEMGARPLRR TLQTQVEDKL
SELLLTGDLM TGQTLKVGVK AGQLKFEVA
//
