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
//