ID A0A0R2CE91_9LACO Unreviewed; 822 AA.
AC A0A0R2CE91;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KRM90063.1};
GN ORFNames=FC80_GL001400 {ECO:0000313|EMBL:KRM90063.1};
OS Liquorilactobacillus cacaonum DSM 21116.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423729 {ECO:0000313|EMBL:KRM90063.1, ECO:0000313|Proteomes:UP000051131};
RN [1] {ECO:0000313|EMBL:KRM90063.1, ECO:0000313|Proteomes:UP000051131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21116 {ECO:0000313|EMBL:KRM90063.1,
RC ECO:0000313|Proteomes:UP000051131};
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:KRM90063.1}.
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DR EMBL; AYZE01000016; KRM90063.1; -; Genomic_DNA.
DR RefSeq; WP_057829625.1; NZ_AYZE01000016.1.
DR AlphaFoldDB; A0A0R2CE91; -.
DR STRING; 1423729.FC80_GL001400; -.
DR PATRIC; fig|1423729.3.peg.1421; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051131; 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 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.
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|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000051131};
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 COILED 411..468
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 822 AA; 91553 MW; 7D7743012233A17B CRC64;
MDNLFTPSAK KVLVLAQEQA KYFRHQAIGT EHLLLALTLE EHGIAAKVLK QFIVTETDVR
EEIERIAGYG TLKNTDKVGY LPYSPRAKEI LALAGDEAKR TNAQKIGTEH LLLALLKNND
ILSSRILQAL NVDTRRMYQS IIHKLGLSEA QMKKFEKKAT KVSGTPTLNS LARDLTDLAQ
NKKIDPVIGR EKEVKRLVQV LSRRTKNNPV LLGEPGVGKT AVAEGLAEAI VAGNVPESLQ
DKRVMMLDMG SLVAGTKYRG EFEDRVKKII DEIYADGNVI LFIDELHTLI GAGGAEGAID
ASNILKPALA RGEVQVVGAT TLDEFQKYIE SDSALERRFA KVMIEEPTSE DTVEILKGLR
SRYEEHHQVE ITDEAIKSAV QLSVRYIADR FLPDKAIDLM DEAAARVRIE NSDGKNKVAD
KRNQLRDLAE EKIVALGAEK FDEAAQIRKK ELKVKKQLET LLENEENKNS GYSLSVNAED
VAKIVSEWTG VPVTQMQKKE TERLIDLEKV LHKRVIGQND AVSAVSRAIR RARSGLKDPN
RPIGSFMFLG PTGVGKTELA KSLAEVIFGS EDSMIRIDMS EYMEKYATSR LIGSPPGYVG
YEEGGQLTEK VRQHPYSVIL FDEVEKAHPD VFNILLQVLD DGYLSDSKGR KIDFRNTIII
MTSNLGATTL RDEKEVGFGS SDASNDFKKM SAKIHEVLKK AFKPEFLNRI DETIIFHALQ
KDELHQIVKL MANELLNRVR EQNVTIKITP AAVDVITKNG FDPEYGARPI RRALQTDVED
KLSELLITGQ IKVGSKVSIG AMKGKINIVI AENEEIKELT KQ
//