ID A0A6I2GBJ9_9LACT Unreviewed; 867 AA.
AC A0A6I2GBJ9;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE SubName: Full=AAA domain-containing protein {ECO:0000313|EMBL:MRI84596.1};
GN ORFNames=GIY09_01625 {ECO:0000313|EMBL:MRI84596.1};
OS Fundicoccus ignavus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Fundicoccus.
OX NCBI_TaxID=2664442 {ECO:0000313|EMBL:MRI84596.1, ECO:0000313|Proteomes:UP000430975};
RN [1] {ECO:0000313|EMBL:MRI84596.1, ECO:0000313|Proteomes:UP000430975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS4759 {ECO:0000313|EMBL:MRI84596.1,
RC ECO:0000313|Proteomes:UP000430975};
RA Siebert A., Huptas C., Wenning M., Scherer S., Doll E.V.;
RT "Characterisation of Fundicoccus ignavus gen. nov. sp. nov., a novel genus
RT of the family Aerococcaceae isolated from bulk tank milk.";
RL Submitted (NOV-2019) 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 -!- 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:MRI84596.1}.
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DR EMBL; WJQS01000001; MRI84596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6I2GBJ9; -.
DR Proteomes; UP000430975; 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; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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:UP000430975};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 1..28
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 76..103
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 440..518
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 867 AA; 98735 MW; A47D5B55C284E431 CRC64;
MTVYTNQVQD ALAKAKELAQ ENQQIQVDIP HLWNVLLQPQ HYALDFYESF ELDINEFIQV
IQKELEKLPV SRSKEIQHAQ QNTPRYDRLL EQAQEEANKL RDEVCSTEHL LLAIMKQSYN
PITVYLTTNQ VDYERLLTQL TKNRKGKRAT QTNQESIYQA LDQYSENLNK KYREGKLDRI
IGRHREIEEV IRVLSRKTKN NAILIGLPGV GKTAIVEGLV QKIEQAQVPD NLLDKEVYNL
DMSSLIAGAK YRGEFEERLK AVLNDVRDSK GKIILFIDEI HTIVGAGKTE GSMDAGNILK
PMLARGELRC IGATTQDEYR ENIEKDKALE RRFQRIIVSE PSIDEATEIL SGIKESYELY
HGVTISEAAV KAAVTLSNRY ITDRFLPDKA IDLMDEASAV RRIQMKSLPE QIQQIKDEII
RLTIEQIKRS DSANSDKPEA VASRQALEQL KDELVEKQDQ WQKEQALISQ LQTLAEDQAA
QFKQAQEALR MGQLEEFVEL TEISLAAIQQ EIAAIEAERR QSTPEALVLI RNQVEEADIA
EVVERQTGIK VQGVMANERQ RLLKLDQIIK ETVVGQDEPV EKVAQAIIRS RAGVQNPNHP
IGSFLFLGPT GVGKTQLAKS LAAVLFGSEL EMIRLDMSEY MEKHAVAKLV GSPPGYVGYE
EGGHLTEAVR HRLYSVVLLD EIEKAHPDVF NILLQVLDEG RLTDSQGRTI DFKNTILIMT
SNIGSLQLLE SLETNHEVTE ATKTAVREEL KQHFRPEFLN RIDSIQLFNP LTLNNMYNIV
ELMLQDLGQR LKRHRIDLVV SAEAKRWLAD KGYDPTLGAR PLQRFIIEQL ETPLAQELIR
QDIQSDTWAH VQLTHDRLTF SYTPKQS
//