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Database: UniProt
Entry: S9SAR6_9RHOB
LinkDB: S9SAR6_9RHOB
Original site: S9SAR6_9RHOB 
ID   S9SAR6_9RHOB            Unreviewed;       873 AA.
AC   S9SAR6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=Salmuc_01016 {ECO:0000313|EMBL:EPX83354.1};
OS   Salipiger mucosus DSM 16094.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX83354.1, ECO:0000313|Proteomes:UP000015347};
RN   [1] {ECO:0000313|Proteomes:UP000015347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX   PubMed=25197501; DOI=10.4056/sigs.4909790;
RA   Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT   strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT   clade.";
RL   Stand. Genomic Sci. 9:1331-1343(2014).
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   -!- 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|ARBA:ARBA00004496,
CC       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:EPX83354.1}.
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DR   EMBL; APVH01000016; EPX83354.1; -; Genomic_DNA.
DR   RefSeq; WP_020042828.1; NZ_KE557275.1.
DR   AlphaFoldDB; S9SAR6; -.
DR   STRING; 1123237.Salmuc_01016; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_5; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000015347; 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: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:UP000015347};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   873 AA;  96376 MW;  5A87074F3773251E CRC64;
     MNLEKFTERS RGFIQAAQTI AMRESHQRLA PEHLLKALLD DDQGLAANLI TRAGGASKRV
     VDALEQRLAK IPKVGGDAGQ VYLDQQTGKV LDEAEKIATK AGDSFVPVER ILMALAMVKS
     PAKEALEAGD VSAQKLNEAI NDIRKGRTAD SANAEEGYDA LKKYAIDLTE RAEQGKIDPI
     IGRDEEIRRA MQVLSRRTKN NPVLIGEAGV GKTAIAEGLA LRIVNRDVPE SLENKRLLAL
     DMGALIAGAK YRGEFEERLK AILKEIESAA GEVILFIDEM HTLVGAGKAD GAMDASNLLK
     PALARGELHC VGATTLDEYR KHVEKDPALA RRFQPVMVQE PTVEDTISIL RGIKEKYELH
     HGVRISDSAL VSAATLSHRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ELDQLDRNIL
     QMQIEQEALK KEDDAGSKDR LEKLEKELAD LQERSAEMTA KWQAERDKLA GARELKEQLD
     KARAELDIAK REGNLARAGE LSYGIIPQLE TQLSEAEAAE EEGDVMVEEA VRPEQIAQVV
     ERWTGIPTSK MLEGERDKLL RMEDGLHKRV VGQNQAVRAV ANAVRRSRAG LNDENRPLGS
     FLFLGPTGVG KTELTKAVAE FLFDDDSAMV RIDMSEFMEK HSVARLIGAP PGYVGYDEGG
     VLTEAVRRRP YQVVLFDEVE KAHPDVFNVL LQVLDDGVLT DGQGRTVDFK QTLIVLTSNL
     GSQALSQLPE GADSAQAKRD VMDAVRAHFR PEFLNRLDEM IVFDRLKRED MGGIVEIQLA
     RLLKRLAARK VRLELDEDAK AWLADEGYDP VFGARPLKRV IQRALQDPLA EMLLAGDIHD
     GDTVPVSAGT DGLLIGDRVA STNRPRPDDA VVH
//
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