ID A0A0R1RBH0_9LACO Unreviewed; 591 AA.
AC A0A0R1RBH0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ATP-dependent Clp protease {ECO:0000313|EMBL:KRL54017.1};
GN ORFNames=FD35_GL000720 {ECO:0000313|EMBL:KRL54017.1};
OS Furfurilactobacillus rossiae DSM 15814.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Furfurilactobacillus.
OX NCBI_TaxID=1114972 {ECO:0000313|EMBL:KRL54017.1, ECO:0000313|Proteomes:UP000051999};
RN [1] {ECO:0000313|EMBL:KRL54017.1, ECO:0000313|Proteomes:UP000051999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15814 {ECO:0000313|EMBL:KRL54017.1,
RC ECO:0000313|Proteomes:UP000051999};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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 -!- 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:KRL54017.1}.
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DR EMBL; AZFF01000012; KRL54017.1; -; Genomic_DNA.
DR RefSeq; WP_017262383.1; NZ_AZFF01000012.1.
DR AlphaFoldDB; A0A0R1RBH0; -.
DR STRING; 1114972.FD35_GL000720; -.
DR PATRIC; fig|1114972.6.peg.721; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 2144783at2; -.
DR Proteomes; UP000051999; 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; 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; IPR001270; ClpA/B.
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 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:KRL54017.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KRL54017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051999};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 44..182
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 315..477
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 484..572
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 591 AA; 66350 MW; 1E5268C438B1948A CRC64;
MPESFLNIFT TNLTAAATAN PDNYLTIGRH QEIEQLVDNL SRKTKNNPLL IGEPGVGKTA
IVDGLARLIA LKKAGPKLND KIIRVLQMAE LRNPTVGTGD AMANFEQLIK ELAASQGKII
LFVDEAHMIM STGDYGDVLK PVMARGEIQL IGCTTLREYH RDIEEDGALK RRFQVIDVPE
PSAQETEAIL TGIKGGYERF HHVTYSDAIV KLCVQLSMRY IPTQFLPDKA IDLLDMSGAV
VSSQQRQAVT ATDVAKVLEM MTHIPITSIL MQDSERLRQL PSNLRQRVIG QDEAIKSVTD
TVVRAKVGIQ DPRLPLGSFF FMGMTGTGKT ELAKALTTAL FDNEQAMIRM DMSEFSLAKS
VDRFQFQLTE KIKHQPYSVV TLDEFEKSNP LVQDRLLQVL GDGELSDEYG QDVDFRNCII
IMTSNIGYEA VNDQADFMSD EKADKFTIQR QKKNFKTIIQ DTLTTNFRPE FVNRIGKVVV
FNMLDKAIIR KIADKDLQEL NVWMKHTGFQ LRYKDDLLNF LADIGTDIKQ GARPLARQID
QEVATPVSYS ILSNKGKGFN VIRIHVSGHG EYGNIRGDRV VHFELINPRL Q
//