ID A0A2U2NAW1_9BIFI Unreviewed; 889 AA.
AC A0A2U2NAW1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PWG66139.1};
GN ORFNames=DF196_04830 {ECO:0000313|EMBL:PWG66139.1};
OS Bifidobacterium callitrichidarum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2052941 {ECO:0000313|EMBL:PWG66139.1, ECO:0000313|Proteomes:UP000245876};
RN [1] {ECO:0000313|EMBL:PWG66139.1, ECO:0000313|Proteomes:UP000245876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRI 5 {ECO:0000313|EMBL:PWG66139.1,
RC ECO:0000313|Proteomes:UP000245876};
RX PubMed=29116036; DOI=10.1099/ijsem.0.002472;
RA Modesto M., Michelini S., Sansosti M.C., De Filippo C., Cavalieri D.,
RA Qvirist L., Andlid T., Spiezio C., Sandri C., Pascarelli S., Sgorbati B.,
RA Mattarelli P.;
RT "Bifidobacterium callitrichidarum sp. nov. from the faeces of the emperor
RT tamarin (Saguinus imperator).";
RL Int. J. Syst. Evol. Microbiol. 68:141-148(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:PWG66139.1}.
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DR EMBL; QFFM01000008; PWG66139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2NAW1; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000245876; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 517..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 406..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 889 AA; 96464 MW; 3362E7F22D35527F CRC64;
MEQKFTTMAQ EAVGDAIQSA SAAGNAQVET LHVMDALLRQ ENGVTRSLIE AAGGNAQAIG
AAVRNALVAL PSASGSTTSQ PQASRQLTAA IAQAEKEMQA MGDEYVSTEH LLIGIAASKP
NQSAEILEKN GVTAAALRKA VPGVRGGAKV TSPDAEGSYK ALEKYSTDLT AAAKEGKLDP
VIGRDQEIRR VIQILSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVAGDVP TTLQGKKLIS
LDLGSMVAGS KYRGEFEERL KAVLNEIKNA NGQIITFIDE IHTIVGAGAA EGSMDAGNML
KPMLARGELR LIGATTLDEY RENIEKDPAL ERRFQQVYVG EPSVEDTIAI LRGLKQRYEA
HHKVTIGDDA LVAAATLSNR YISGRQLPDK AIDLVDEAAA HLRMELDSSP EEIDELQRKV
TRLEMEEMQL KKAEDPASKE RLGKLQAELA DTREKLSGLK ARWDAEQAGH NKVGELRAKL
DDLRVQADKF TREGNLAEAS KILYGEIPAI QKELSAAENA DAEAKDTGST DPANEPMVPD
RVDADSVAEI VSDWTGIPVG RLMQGENEKL LHMEDYLGKR VIGQKEAIQA VSDAVRRSRA
GISDPNRPTG SFLFLGPTGV GKTELAKALA DFLFDDEKAM VRIDMSEYME KASVSRLIGA
APGYVGYEQG GQLTEAVRRR PYSVVLFDEV EKANPEIFDV LLQVLDDGRL TDGQGRTVDF
KNTILIMTSN LGSQFLVNED MDPDAKKKAV MDAVHMNFKP EFLNRLDDIV MFHPLTREEL
GGIVDIQVKS VAQRLTDRRI TLDVTDSARE WLANTGYDPA YGARPLRRLV QTEVGDQLAR
MLLAGKVHDG DTVLVDQTGG EHLELSAWAS DQIVGDDPDV NVDDVTADK
//