ID A0A1Z5ICA6_9LACO Unreviewed; 828 AA.
AC A0A1Z5ICA6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ATP-dependent Clp protease ATP-binding protein {ECO:0000313|EMBL:GAW99278.1};
GN Name=clpA_3 {ECO:0000313|EMBL:GAW99278.1};
GN ORFNames=IWT30_01239 {ECO:0000313|EMBL:GAW99278.1};
OS Secundilactobacillus mixtipabuli.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1435342 {ECO:0000313|EMBL:GAW99278.1, ECO:0000313|Proteomes:UP000198374};
RN [1] {ECO:0000313|EMBL:GAW99278.1, ECO:0000313|Proteomes:UP000198374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IWT30 {ECO:0000313|EMBL:GAW99278.1,
RC ECO:0000313|Proteomes:UP000198374};
RA Tohno M., Tanizawa Y., Arita M.;
RT "Draft genome sequences of new species of the genus Lactobacillus isolated
RT from orchardgrass silage.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:GAW99278.1}.
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DR EMBL; BCMF01000005; GAW99278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5ICA6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198374; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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};
KW Hydrolase {ECO:0000313|EMBL:GAW99278.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:GAW99278.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198374};
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..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 92068 MW; FA5485EB435CB91B CRC64;
MDNLFTPSAK SVLALAQEQA KYFKHQAVGT EHLLLALTIE KNGIANKVLQ QFSISEDDVR
EEIERFTGYG TLSNVDKDTY LPYSPKAKDM LSVAGEEAKR IGATKIGTEH LLLALLSDET
ILSSRILMNL NIDLAQARKV IMRKLGVTEN QDKRRNQRGR KQQGGTPTLD SLARDLTQLA
RDDRMDPTVG RNNEVRRVIQ ILSRRTKNNP VLIGEPGVGK TAIAEGLAQR IVKGDVPEDM
QNKRLMALDM GSLVAGTKYR GEFEDRLKKV IEEIYNDGEV ILFIDELHTL IGAGGAEGAI
DASNILKPAL ARGELQTIGA TTLDEYQKYI ESDAALERRF ATVQVNEPTE DETIEILKGL
RPRYEQHHKA NISDEALEQA VKLSSRYITE RYLPDKAIDL MDEAAAKVRI SQMDKPNNQT
KQEAKLSDLS DQREAAILDQ RFEEAAKIRE QEIALKDKLD KKAEKQAETG AKYNLNVTGE
DVAEVVSEWT GVPTTQLNQT EQNRLVNLEG ILHKRVVGQE EAVSAVSRAI RRARSGLKDP
NRPIGSFMFL GPTGVGKTEL AKALAEAMFG SEDNMIRVDM SEYMEKYSTS RLIGSAPGYV
GYDEGGQLTE KVRQKPYSVV LFDEVEKAHP DVFNLLLQVL DDGFLTDSKG RKVDFRNTIL
IMTSNLGATR LRDEKTVGFG AEDKSGDYTA MASTIRETLK QSFRPEFLNR IDEVVIFHSL
KKKELHQIVK LMAKTVIDRV KAQGINIKVT PAAIDVIADA GFDPEYGARP IRRALQTKVE
DRLSEAMLSG EIQAGNMVTL GASRGKITLN VKQPEKTENK TNETVGSK
//
