ID A0A0R2A3C1_9LACO Unreviewed; 824 AA.
AC A0A0R2A3C1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KRM61479.1};
GN ORFNames=FC26_GL001553 {ECO:0000313|EMBL:KRM61479.1};
OS Paucilactobacillus vaccinostercus DSM 20634.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM61479.1, ECO:0000313|Proteomes:UP000051733};
RN [1] {ECO:0000313|EMBL:KRM61479.1, ECO:0000313|Proteomes:UP000051733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM61479.1,
RC ECO:0000313|Proteomes:UP000051733};
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 -!- 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:KRM61479.1}.
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DR EMBL; AYYY01000025; KRM61479.1; -; Genomic_DNA.
DR RefSeq; WP_057778668.1; NZ_AYYY01000025.1.
DR AlphaFoldDB; A0A0R2A3C1; -.
DR STRING; 1423813.FC26_GL001553; -.
DR PATRIC; fig|1423813.3.peg.1580; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051733; 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 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.
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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000051733};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 424..459
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 146..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 420..466
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 157..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 91847 MW; C7B4FC7948E3C123 CRC64;
MDNLFTPSAK NVLVLAQEQA KYFKHQAVGT EHLLLALSIE QNGIANKVLQ QFSITEDDIR
EEIERFTGYG TLTNIDKDTY LPYSPKAKEI LAAAGDEAKR LGAVKIGTEH LLLALLTDDS
ILSSRILLNL NVDLNQTRKN VLRRLGVADT TKRHQNNRAK NPQPQGTPTL DSLARDLTQS
AREDKMDPVV GREQEVRRVI QILSRRTKNN PVLIGEPGVG KTAIAEGLAQ RIVAGNVPDD
LASKRIMMLD MGSLVAGTKY RGEFEDRLKK VIDEIYHDGH VILFIDELHT LIGAGGAEGA
IDASNILKPA LARGELQTIG ATTLDEYQKY IESDAALERR FATVQVDEPT EDEAVAILKG
LRGRYEDHHK AEITDEAIIQ AVKLSSRYIS DRFLPDKAID LMDEAAAKVR IDAEDKPSKK
TKQVDKLEQL RQDKEKAIEE QNFDLAAEIR QQELKLKEKV DQQAEKDKTN RQYDLQVSEE
DVAQVVAEWT GIPLTQLRKT ESERLVNLEK ILHERVIGQE EAVSAVARAI RRARSGLKDP
NRPIGSFMFL GPTGVGKTEL AKALAEAMFG SEDNMIRVDM SEYMEKYSTS RLIGAAPGYV
GYDEGGQLTE KVRQHPYSVV LLDEAEKAHP DVFNLLLQVL DDGYLTDAKG RKVDFRNTIL
IMTSNLGATA LRDEKEVGFG AKDVQSDYRA MAGAITEQLK MHFRPEFLNR IDETIIFHSL
KKDELHQIVK LMSHDLVKRV AEQAITLKFT SAAIDVVAKA GFDPEYGARP IRRALQTEVE
DRLSEAMLGG QIKIGDTVVV GSTRGKIKVS VQDDQHNSRL ITTN
//
