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Database: UniProt
Entry: A0A2S8SS39_9BACT
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ID   A0A2S8SS39_9BACT        Unreviewed;       886 AA.
AC   A0A2S8SS39;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=B1R32_11087 {ECO:0000313|EMBL:PQV63621.1};
OS   Abditibacterium utsteinense.
OC   Bacteria; Abditibacteriota; Abditibacteriia; Abditibacteriales;
OC   Abditibacteriaceae; Abditibacterium.
OX   NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV63621.1, ECO:0000313|Proteomes:UP000237684};
RN   [1] {ECO:0000313|EMBL:PQV63621.1, ECO:0000313|Proteomes:UP000237684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV63621.1,
RC   ECO:0000313|Proteomes:UP000237684};
RX   PubMed=29475572;
RA   Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.;
RT   "Abditibacterium utsteinense sp. nov., the first cultivated member of
RT   candidate phylum FBP, isolated from ice-free Antarctic soil samples.";
RL   Syst. Appl. Microbiol. 0:0-0(2018).
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:PQV63621.1}.
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DR   EMBL; NIGF01000010; PQV63621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8SS39; -.
DR   InParanoid; A0A2S8SS39; -.
DR   Proteomes; UP000237684; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:PQV63621.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PQV63621.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237684};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          5..156
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          422..546
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   886 AA;  98235 MW;  E61A055F0B6F6FB0 CRC64;
     MAIDFNKWTT KAQEALESAR DLAVEYGHQE MDVEHLFLSL LRQNEGTTAP VLGKIGASAA
     TSGRELEAEL ARRPKVSGAE LGRGLTIRLG GNGRDGQGGV LGAAQKSAGQ LKDEFLSTEH
     LLLGISEDKG FSGGLLKTHG ATRDAILQAL AQIRGGQRVT DQNPEEKYQA LEKFTRDLTA
     EAARGKLDPV IGRDEEIRRV MQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRVASGDVPE
     TLKDKKVLSL DLGALIAGAK YRGEFEDRLK AVLKEIERSN GQIVLFIDEI HTLVGAGAAE
     GAVDAANLLK PMLARGELRC VGATTLEEYR KYIEKDAALE RRFQPIYVGE PSVEDTIAIL
     RGLKDRYEVH HKVRIKDSAL VAAAVLSNRY LTERFLPDKA IDLVDEAASK LRIEIASMPT
     EIDEILRRIM QLEIEREALS RETKGVNLFG NRASDATRER QQVIEKQLAE LKEQSSQLRA
     QWQSEKDAIG HVSSLKEELE NVQFEIERAT QAADLGRAAE LRYGKLPELQ RELETETLKL
     QERQSQGQML KEEVDEEDIA EVVGKWTGIP ISRLVESEVQ KLLHMEENLR GRVVGQDTAL
     EAVADAVRRS RAGLSDPNKP LGSFLFLGPT GVGKTELARG LAEFLFDDER AMVRLDMSEY
     MEKHSVSRLI GAPPGYVGYE EGGQLTEAVR RRPYSVVLFD EIEKAHPDVF NALLQLLDDG
     RLTDGQGRVV SFKNTVVIMT SNLASSLIMS AEADDFTLKD RVFEQLRAHF RPEFLNRIDE
     IVLFESLKRE QLGRIVEIQL EGLRKRLAER GITLTLTESA KNVVGEEGYD PQFGARPLKR
     AIQRLIQDPL SKKILSGEIR DGQSVEIDAG HEGQLIFRPA EETIAV
//
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