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Database: UniProt
Entry: A0A0R1RBH0_9LACO
LinkDB: A0A0R1RBH0_9LACO
Original site: A0A0R1RBH0_9LACO 
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
//
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