ID A0A0R2ARE1_9LACO Unreviewed; 826 AA.
AC A0A0R2ARE1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KRM68260.1};
GN ORFNames=FD06_GL001281 {ECO:0000313|EMBL:KRM68260.1};
OS Apilactobacillus ozensis DSM 23829 = JCM 17196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Apilactobacillus.
OX NCBI_TaxID=1423781 {ECO:0000313|EMBL:KRM68260.1, ECO:0000313|Proteomes:UP000052012};
RN [1] {ECO:0000313|EMBL:KRM68260.1, ECO:0000313|Proteomes:UP000052012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23829 {ECO:0000313|EMBL:KRM68260.1,
RC ECO:0000313|Proteomes:UP000052012};
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:KRM68260.1}.
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DR EMBL; AYYQ01000029; KRM68260.1; -; Genomic_DNA.
DR RefSeq; WP_056966141.1; NZ_AYYQ01000029.1.
DR AlphaFoldDB; A0A0R2ARE1; -.
DR STRING; 1423781.FD06_GL001281; -.
DR PATRIC; fig|1423781.4.peg.1327; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000052012; 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:SF193; CHAPERONE PROTEIN CLPB; 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|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000052012};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 427..462
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 423..480
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 826 AA; 91708 MW; F6BE68BB0BCA3E29 CRC64;
MNNNNIFTPS AKNVLILAQE QAKGFKHQAI GTEHILLALT MEKNGIAYSA LQHFSVNEED
IRGEIERIAG YGNFVDADND TYLPYSPKAQ NVIAMSGQIA KQYGALKVGT EHLLLALLSD
NALIASRILF SLDVKPSEVQ KVTFRKMGVS SASAKRMQYR NKNKRNEGPT PTLDSLARDM
TEIAKQGGMD PTIGRDKEVR RVIQILSRRT KNNPVLIGEP GVGKTAIAEG LAQKMVAGEV
PGDMANKRLM MLDMGSLVAG TKYRGEFEDR LKKVINEIRE DGHVILFIDE LHTLIGAGGA
EGAIDASNIL KPALARGELQ TIGATTLDEY QKHIESDQAL ARRFATVMVN EPTPEQTKQI
LSGLRPKYEK HHHVKITDEA IDEAVKLSTR YISNRFLPDK AIDLMDEAAA KIRIDSMGKS
NRLAAKQKEL NQLSRQMELA IENQEFEKAV QIRQAEKKLQ DELENLKERA EKKNQTENDN
YSLTETGEDI ANIVHEWTGI PVNQMTKSDS AKLVNLEKIL HKKIVGQDEA VSAIARAIRR
ARSGLKNPNR PIGSFIFLGP TGVGKTELAK DLAETMFGSK DDMIRVDMSE YMEKYSTSRL
VGSAPGYVGY DEGGQLTEKV RQHPYSVVLF DEVEKAHPDV FNLLLQVLDD GYMTDSKGRK
VDFRNTLLIM TSNLGATALR DKKTVGFGAE SADENSFEAM SSVIKAQLKK HFKPEFLNRI
DETVIFHSLK KPQIRQIVKL NLKDLIARVE EQGIEIKFTP AAIDVIAKAG FDPEYGARPI
RRAIQTQVED KVSEMILSGD LSAGSTLSIG SHKGKLTFNN KETVKQ
//
