ID R5UVP2_9BACT Unreviewed; 863 AA.
AC R5UVP2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BN709_01660 {ECO:0000313|EMBL:CCZ82388.1};
OS Odoribacter laneus CAG:561.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC Odoribacter.
OX NCBI_TaxID=1263089 {ECO:0000313|EMBL:CCZ82388.1, ECO:0000313|Proteomes:UP000017974};
RN [1] {ECO:0000313|EMBL:CCZ82388.1, ECO:0000313|Proteomes:UP000017974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:561 {ECO:0000313|Proteomes:UP000017974};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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}.
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:CCZ82388.1}.
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DR EMBL; CBAQ010000104; CCZ82388.1; -; Genomic_DNA.
DR RefSeq; WP_009137653.1; NZ_HF997812.1.
DR AlphaFoldDB; R5UVP2; -.
DR Proteomes; UP000017974; Unassembled WGS sequence.
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:0003723; F:RNA binding; 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; IPR017729; ATPase_T6SS_ClpV1.
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 InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR NCBIfam; TIGR03345; VI_ClpV1; 1.
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; PS50302; PUM; 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:UP000017974};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 403..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 97080 MW; F52284B8280E8F3F CRC64;
MNTDNYTIKS QEALQKAVQL AQAKGQQAIE TGHLLKAVVE VGENVTHFIF NKLGVNSNNL
LSALDRIIDT YPRVSGGEVY LSSDANRVLE KATRFASEMG DQYISLEHIL LGLLEGRDQV
AQLMKDSGMT EKETKAAIGE LRKGSKVNSQ SAESTYDSLG RFAINLNERA RNGKLDPVIG
RDDEIRRVLQ ILSRRTKNNP ILIGEPGVGK TAIAEGLAQR IVNGDVPSNL ASKQIYSLDM
GALIAGAKYK GEFEERLKAV VNEVISSEGE IILFIDEIHT LVGAGKSDGA MDAANILKPA
LARGDLRAIG ATTLNEYQKY FEQDKALERR FQKVMIDEPD VMSAISIMRG LKERYENHHK
VRITDDAIIA SVELSHRYIS DRFLPDKAID LVDEAAARLR LEMNSVPEEI DELDRKIQQL
QIEKEALKRE GSSKKLDDIK KELADLTEER TKLRAQWESE RSLIDEIQKN KDAIEQYKFE
ATRAERDGDY GKVAELRYGK IKEAEGRIEE VKQKLADMKN GESLIREEVT ADDIATVVSK
WTGIPVNRMM QSERQKLLSL EQELHRRVVG QDVAIAALAD AVRRNRAGLQ DAKRPIGSFI
FLGTTGVGKT ELAKALAEFL FDDESQMTRI DMSEYQERHS VSRLIGAPPG YVGYDEGGQL
TEAVRRKPYS VILLDEIEKA HPDVFNILLQ VLDDGRLTDN KGRVVDFKNT IIIMTSNIGA
HIIQEKLKDL NEKNRDEIVE KTNAEVYEML KQTIRPEFLN RIDEVIMFTP LQKNEIVDIV
RLQINGVNKM LANNGILLEV TDKAVEWIAN EGYDPQFGAR PVKRIIQRTL LNDLSKQILS
EKVSKDNHIV VDVKNNEIVF RNK
//