ID I0IRT5_LEPFC Unreviewed; 863 AA.
AC I0IRT5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=LFE_2312 {ECO:0000313|EMBL:BAM07984.1};
OS Leptospirillum ferrooxidans (strain C2-3).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM07984.1, ECO:0000313|Proteomes:UP000007382};
RN [1] {ECO:0000313|EMBL:BAM07984.1, ECO:0000313|Proteomes:UP000007382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-3 {ECO:0000313|EMBL:BAM07984.1,
RC ECO:0000313|Proteomes:UP000007382};
RX PubMed=22815442; DOI=10.1128/JB.00696-12;
RA Fujimura R., Sato Y., Nishizawa T., Oshima K., Kim S.-W., Hattori M.,
RA Kamijo T., Ohta H.;
RT "Complete Genome Sequence of Leptospirillum ferrooxidans Strain C2-3,
RT Isolated from a Fresh Volcanic Ash Deposit on the Island of Miyake,
RT Japan.";
RL J. Bacteriol. 194:4122-4123(2012).
RN [2] {ECO:0000313|Proteomes:UP000007382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382};
RA Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M.,
RA Kamijo T., Ohta H.;
RT "The complete genome sequence of the pioneer microbe on fresh volcanic
RT deposit, Leptospirillum ferrooxidans strain C2-3.";
RL Submitted (MAR-2012) 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. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; AP012342; BAM07984.1; -; Genomic_DNA.
DR RefSeq; WP_014450467.1; NC_017094.1.
DR AlphaFoldDB; I0IRT5; -.
DR STRING; 1162668.LFE_2312; -.
DR GeneID; 78149966; -.
DR KEGG; lfc:LFE_2312; -.
DR PATRIC; fig|1162668.3.peg.2746; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_0; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000007382; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
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; IPR017730; Chaperonin_ClpB.
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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
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|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000007382};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 415..529
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 95491 MW; 15FD13765FAE9CAC CRC64;
MNLEKLTIKS QEALQSAVDE ARRRGNTLVE PIHLLRELLV QEGGLVIPLL EKMGTGQEAL
KAKTDEAIKL LPTVTGSGAG SGPSLSRSTG DLLDRAQEEA KTFKDDFVSV EHILLAMIGG
SGTESKLLKG AGLDREKVMK ALTEVRGNQR VTDQNPEDKY QALSKFGRDL TAMAKQNKLD
PVIGRDAEIR RVVQVLSRRT KNNPVLIGDP GVGKTAIVEG LAQRIVSGDV PEGLKDRTIF
ALDLGSLLAG AKYRGDFEER LKAVLKEVTG SDGRIILFID ELHTIVRAGA TEGGAMDASN
LLKPALARGE LRAIGATTLD EFREHIEKDA ALERRFQPVL VGEPSIEDTI AILRGLKEKY
EIHHGVRIRD SAIVAAAVLS QRYISGRFLP DKAIDLIDEA ASQLRVAIDS MPRTLDDVDR
RIRQLEMEKM ALAKEEDTES LGRRQEVENE LESKKSELAR LKVQWDGEKK DIGTVRTLKQ
QIEEARQAME MAIREGSFDR ASEIQYSRIP KLEKELADSQ KLLENQGNRL LKEEVEEEDV
ADVISRWTGI PVSRMLEGEV QKLLQMEERL GSRVVGQQEA LAAVSNAIRR ARAGIQDPNR
PLGSFFFLGP TGVGKTELAK ALAEFLFDSD QAMIRIDMSE YMEKHAVSRL VGAPPGYVGY
EEGGQLTESI RRKPYSVILL DEVEKAHPDV FNILLQVLDD GRLTDGQGRV VDFRNTVIIM
TSNVGSDIIR ERVGLDADET KQEVLEILSK TFRPEFLNRI DEIIVFHPLL RHEIGRIVRI
QLDGLNARLK DQGIQLEISP AAEEELTAVG YDPVYGARPL KRAVQSLILN PLAQKILSGG
ISQGSVVSVD FDGIDFTFRP HGT
//