ID B1XWY7_LEPCP Unreviewed; 916 AA.
AC B1XWY7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Type VI secretion ATPase, ClpV1 family {ECO:0000313|EMBL:ACB36336.1};
GN OrderedLocusNames=Lcho_4084 {ECO:0000313|EMBL:ACB36336.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB36336.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB36336.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) 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|ARBA:ARBA00008675}.
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DR EMBL; CP001013; ACB36336.1; -; Genomic_DNA.
DR RefSeq; WP_012349079.1; NC_010524.1.
DR AlphaFoldDB; B1XWY7; -.
DR STRING; 395495.Lcho_4084; -.
DR KEGG; lch:Lcho_4084; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_1_1_4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000001693; Chromosome.
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; IPR017729; ATPase_T6SS_ClpV1.
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; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03345; VI_ClpV1; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 158..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 99913 MW; DBEDD6D7519FC788 CRC64;
MTEISRTALF GKLDPLAYKA IEGATVFCKM RGNPYVELQH WLAQILNTPD SDLHRIIRHY
ELDSAALAAD LTRSLDRLPR GASSISDFST FVLDAVERAW IYGSLMFGER QIRTGHLLIG
LLKTPSLRNV LLSISKQFER VKLDDLADRF ASLLAASPEQ SQGASDSGAA PGEASDAIPP
AAMGKQEALK RFTTDLTEQA RAGKMDPIVG RDDEIRQVVD ILMRRRQNNP ILVGEAGVGK
TAVVEGFAQR IARGDVPPAL KEVQLLALDV GLLQAGASMK GEFEQRLRSV IEEVQASPKP
IILFVDETHT LVGAGGAAGT GDAANLLKPA LARGTLRTVG ATTFAEYKKY IEKDPALTRR
FQSVQVDEPD EKRAILMMRG VASTMEKHHQ VQILDEALEA AVKLSHRYIP ARQLPDKSVS
LLDTACARVA VSLHATPAEV DDTRKRIEAL ETELGIIGRE RAIGIDVLER EADASRLLAD
ERERLALLDQ RWAEEKTLVD ELLALRAKLR GGVRPVEGTG SELEAAVAPV AEGVAEPGLS
EGERADALAR LREVQAQLAT LQGESPLILP TVDYQAVASV VGDWTGIPVG RMARNEIDTV
LKLPTLLAQR VIGQDHAMEM IAKRIQTSRA GLDNPGKPIG VFMLAGTSGV GKTETALALA
EALYGGEQNL IVINMSEYQE AHTVSSLKGA PPGYVGYGEG GVLTEAVRRK PYSVVLLDEV
EKAHPDVHEL FFQVFDKGFM EDGEGRVIDF KNTLILLTTN AGTELISALC RDPARMPDPE
GMAKALRQPL LEIFPPALLG RLVAIPYYPL SDEMLGRIVK LQLERIRKRV ETRYKIPFEY
GDDVVELVVS RCTESESGGR MIDAILTNTM LPDISREFLN RMLDGTPIER VEVQVSEGNF
AYGFGPDTAA PARDEP
//
