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Database: UniProt
Entry: A0A0R1Y077_9LACO
LinkDB: A0A0R1Y077_9LACO
Original site: A0A0R1Y077_9LACO 
ID   A0A0R1Y077_9LACO        Unreviewed;       796 AA.
AC   A0A0R1Y077;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KRM32636.1};
GN   ORFNames=FC83_GL000503 {ECO:0000313|EMBL:KRM32636.1};
OS   Agrilactobacillus composti DSM 18527 = JCM 14202.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Agrilactobacillus.
OX   NCBI_TaxID=1423734 {ECO:0000313|EMBL:KRM32636.1, ECO:0000313|Proteomes:UP000051236};
RN   [1] {ECO:0000313|EMBL:KRM32636.1, ECO:0000313|Proteomes:UP000051236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18527 {ECO:0000313|EMBL:KRM32636.1,
RC   ECO:0000313|Proteomes:UP000051236};
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   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {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:KRM32636.1}.
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DR   EMBL; AZGA01000070; KRM32636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1Y077; -.
DR   STRING; 1423734.FC83_GL000503; -.
DR   PATRIC; fig|1423734.3.peg.504; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000051236; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   Gene3D; 4.10.860.10; UVR domain; 1.
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   InterPro; IPR001943; UVR_dom.
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; 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.
DR   PROSITE; PS50151; UVR; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051236};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..116
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          394..429
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
SQ   SEQUENCE   796 AA;  88034 MW;  E6C1CF3F2CF2E89A CRC64;
     MALVLENDGV AGKTLRQLTI TPDDVKEEIE RFTGYGSSNA NPDDQKEAYL PYSPKAKQIL
     TFAGDEAKRL GAMKIGTEHI LLGLLHEDDV LASRIISNLG LSLSKTRQVL LKKMGITEAS
     AKRRVAAPKR RADKQGTPTL DSLARDLTQS AAEGRMDPVV GRDKEVKRVI QILSRRTKNN
     PVLIGEPGVG KTAIAEGLAQ RINDHNVPSD MYNKRLMMLD MGSLVAGTKY RGEFEDRLKK
     VIDEIYQDGN VILFIDELHT LIGAGGAEGA IDASNILKPA LARGELQLIG ATTLDEYQKY
     IERDAALERR FATIQVNEPT PEEAEQILKG LRGRYEEHHG VTITDEALHQ AVVLSSRYIT
     GRFLPDKAID LVDESAAKVR LDAADNLSPS DKLQQQLDSL VTKKEKAIEN QDFEKAANYR
     EDEMALKDKL ASESDAQTDG IRKDIKVTGE DVAQVVSEWT GVPLTQLQKS ESARLVNLES
     ILHKRVVGQE EAISAVARAI RRARSGLKDP NRPIGSFMFL GPTGVGKTEL AKALAEAMFG
     SEDNMIRVDM SEYQEQYTTS RLIGSPPGYV GYDEGGQLTE KVRNKPYSVV LFDEVEKAHP
     DIFNILLQVL DDGYLTDAKG RRVDFRNTIL ILTSNLGATA LRDEKSVGFG AEKASQDYPA
     MRSRIMEEMK RFFRPEFLNR IDETVVFHPL DKDELRQIVK IMSKTVIKRL AEQEIKVKIT
     NAALDAVAAA GFDPEYGARP IRRAIQTQIE DKVSESLLTG QIKSGDSITV GASKGKITVS
     VKEPEDKNKP QDKVKS
//
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