ID H4GKY6_9LACO Unreviewed; 679 AA.
AC H4GKY6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:EHS84838.1};
GN ORFNames=PS3_9730 {ECO:0000313|EMBL:EHS84838.1};
OS Limosilactobacillus gastricus PS3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1144300 {ECO:0000313|EMBL:EHS84838.1, ECO:0000313|Proteomes:UP000004567};
RN [1] {ECO:0000313|EMBL:EHS84838.1, ECO:0000313|Proteomes:UP000004567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS3 {ECO:0000313|EMBL:EHS84838.1,
RC ECO:0000313|Proteomes:UP000004567};
RX PubMed=23846278;
RA Martin V., Cardenas N., Jimenez E., Maldonado A., Rodriguez J.M.,
RA Fernandez L.;
RT "Genome Sequence of Lactobacillus gastricus PS3, a Strain Isolated from
RT Human Milk.";
RL Genome Announc. 1:E00489-E00413(2013).
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:EHS84838.1}.
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DR EMBL; AICN01000076; EHS84838.1; -; Genomic_DNA.
DR AlphaFoldDB; H4GKY6; -.
DR STRING; 1144300.PS3_9730; -.
DR PATRIC; fig|1144300.3.peg.1728; -.
DR Proteomes; UP000004567; 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; 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; 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; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 Hydrolase {ECO:0000313|EMBL:EHS84838.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EHS84838.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004567};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 65..209
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 404..567
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 581..670
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 75940 MW; EBCFBEF28A5C699F CRC64;
MKRLGVSERN MNRSNRQNNQ PAEGTPTLDK LGRDMTKLAN EKDVDPVIGR NKEIQRALQI
LSRRTKNNPV LIGEPGVGKT AIVEGLAQRI VKGSVPETLQ NKRLISLDMG SLVAGTKFRG
EFEDRLKKVI NEIAEDGNVI LFVDEIHTLI GAGGAEGAID ASNILKPALA RGEIQLIGAT
TLDEYRKYVE KDAALERRFS TVMVEEPSTE ETLTILEGLR EQYQQYHQVE ITDDALQSAV
ELSKRYINDR YLPDKAIDLM DESAATIRIN AENHPHKDIQ LSQQLAEVRN QKEQAILEQN
FDLAADLRQS ELKLKVELEA YEVKRQRAAD DGHYRLKVTA NDVATVVAEW TGVPVTQLQK
QESKRLVNLE QNLHQRVIGQ DEAVRVISEA IRRSRSGLKD PQRPIGSFMF LGPTGVGKTE
LAKALAEEMF GSRDQMIRID MSEYMERYST SRLVGAAPGY VGYEEGGQLT EQVRRHPYSV
VLLDEVEKAH PDVFNLLLQV LDDGFLTDSQ GRRVDFRNTI LIMTSNLGAT QLQDTKTVGF
GATDVHEDYA AMKAAVNEQL KLAFRPEFLN RIDETIVFHS LTKPELRQIV KLLASQLIHR
LADQGIKLKL TTAALDTIAE DGYNPAYGAR PLRRSIQKLV ENPMSMLILN GDIQVGDQIT
VGAHKGQLDF KQNGQLVTV
//