ID A0A0R2FHM2_9LACO Unreviewed; 828 AA.
AC A0A0R2FHM2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KRN23892.1};
GN ORFNames=FD14_GL000647 {ECO:0000313|EMBL:KRN23892.1};
OS Secundilactobacillus similis DSM 23365 = JCM 2765.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1423804 {ECO:0000313|EMBL:KRN23892.1, ECO:0000313|Proteomes:UP000051442};
RN [1] {ECO:0000313|EMBL:KRN23892.1, ECO:0000313|Proteomes:UP000051442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23365 {ECO:0000313|EMBL:KRN23892.1,
RC ECO:0000313|Proteomes:UP000051442};
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:KRN23892.1}.
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DR EMBL; AYZM01000087; KRN23892.1; -; Genomic_DNA.
DR RefSeq; WP_054734074.1; NZ_BBAD01000011.1.
DR AlphaFoldDB; A0A0R2FHM2; -.
DR STRING; 1423804.FD14_GL000647; -.
DR PATRIC; fig|1423804.4.peg.694; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051442; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000051442};
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 423..458
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 148..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 419..468
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 828 AA; 91959 MW; 682389CE7572FF03 CRC64;
MDNLFTPSAK SVLALAQEQA KFFKHQAVGT EHLLLALTIE KNGIANKVLQ QFSISEDDVR
EEIERFTGYG TLGNVDKDTY LPYSPKAKDM LSVAGEEAKR IGATKIGTEH LLLALLSDET
ILSSRILMNL NIDLGQARKV ILRKLGVSET QDKRRNPRAR KQQGGTPTLD SLARDLTQLA
KDDRMDPTVG RNKEVRRVIQ ILSRRTKNNP VLIGEPGVGK TAIAEGLAQR IVAGDVPEDM
QQKRLMALDM GSLVAGTKYR GEFEDRLKKV IEEIYNDGQV ILFIDELHTL IGAGGAEGAI
DASNILKPAL ARGELQTIGA TTLDEYQKYI ESDAALERRF ATVQVDEPTE DETIEILKGL
RPRYEEHHHA NISDEALEQA VKLSTRYITD RFLPDKAIDL MDEAAAKVRI SQMDQPSAKS
KQEAKLAELA DQREAAILDQ RFEEAADLRE QEIALKAKLD KKAKKKAESD QQYDLNVTGE
DVAEVVSDWT GVPTTQLQRT EQERLINLEN ILHKRVVGQE EAVSAVSRAI RRARSGLKDP
NRPIGSFMFL GPTGVGKTEL AKALAEAMFG SEDNIIRVDM SEYMEKYSTS RLIGSAPGYV
GYDEGGQLTE KVRQKPYSVV LFDEVEKAHP DVFNLLLQVL DDGYLTDSKG RKVDFRNTIL
IMTSNLGATR LRDEKTVGFG AEDHAEDYKA MAATIRETLK QSFRPEFLNR IDEIVVFHAL
VKKELHQIVK LMAKTVIKRI SDQGIKVKVT PAAIDVIADA GFDPEYGARP IRRALQTKIE
DRLSEALLSG EIKAGNQVTL GATKGEITVN VKQETEKPVE KSQPVGTK
//