ID A0A080N381_9BIFI Unreviewed; 879 AA.
AC A0A080N381;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BBOMB_0966 {ECO:0000313|EMBL:KFF31583.1};
OS Bifidobacterium bombi DSM 19703.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF31583.1, ECO:0000313|Proteomes:UP000028730};
RN [1] {ECO:0000313|EMBL:KFF31583.1, ECO:0000313|Proteomes:UP000028730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF31583.1,
RC ECO:0000313|Proteomes:UP000028730};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(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. {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|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:KFF31583.1}.
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DR EMBL; ATLK01000001; KFF31583.1; -; Genomic_DNA.
DR RefSeq; WP_044086984.1; NZ_JDTS01000002.1.
DR AlphaFoldDB; A0A080N381; -.
DR STRING; 1341695.BBOMB_0966; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000028730; 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 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.
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:UP000028730};
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 72..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..462
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COMPBIAS 72..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 96071 MW; 39B2130C3AA36193 CRC64;
MEQNFTTMAQ SAIGDAVQSA AAAGNPQVDT LHLLDALLRQ ENGVVPGLIE AAGGDRQAIG
AQVRNALVQL PSASGSSTSQ PDASRQLSQT LSEAEKEMKR MGDEYVSTEH LLMGIIDAAP
NEAARILTSH DVTAKALRDA VPKVRGGAKV TSPEAEGNYK ALEKYSTDLT AQAKEGKLDP
VIGRDQEIRR VIQILSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVAGDVP TGLQHKRLIS
LDLGSMVAGS KYRGEFEERL KAVLNEIKSA NGEIITFIDE IHTIVGAGAA EGSMDAGNML
KPMLARGELR LIGATTLDEY RENIEKDPAL ERRFQQVFVG EPSVEDTIAI LRGLKQRYEA
HHKVTIGDDA LVAAATLSNR YISGRQLPDK AIDLVDEAAA HLRMELDSQP EEIDELQRRE
TRLEMEEMQL KKAEDPASKI QLKKLQSELA DTREKLAGLK TRWDAEKAGH NKVGDLRAQL
DAKRVQADKF TREGNLEEAS RILYGEIPAI QKQLDLAEQA ADEQNDSGQE TEPMVPDHVD
ADSVAGIVSE WTGIPVGRLM QGENEKLLHM EDFLSKRVIG QKEAIQAVSD AVRRSRAGIS
DPDRPTGSFM FLGPTGVGKT ELAKALADFL FDDEKAMVRI DMSEYMEKSS VSRLIGAAPG
YVGYDEGGQL TEAVRRRPYS VVLFDEVEKA NPEVFDLLLQ VLDDGRLTDG QGRTVDFKNT
ILIMTSNLGS QFLVQDDLDE DAKREAVMDA AHAHFKPEFL NRLDEMVIFH PLTREELGGI
VDIQVKQVAS RLTDRRITLS VTQAAKSWLA DAGYDPAYGA RPLRRLVQTE VGDQMARMLL
SGAVHDGDTV LVDQTGGEHL ELTVMPSDPL AEDSQEGKA
//
