ID A0A174S0H9_BACUN Unreviewed; 864 AA.
AC A0A174S0H9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB_2 {ECO:0000313|EMBL:CUP91434.1};
GN Synonyms=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:KAB4242228.1};
GN ORFNames=DXD40_08820 {ECO:0000313|EMBL:RGJ93926.1}, ERS852554_02255
GN {ECO:0000313|EMBL:CUP91434.1}, GAP41_11330
GN {ECO:0000313|EMBL:KAB4242228.1}, GAP48_02460
GN {ECO:0000313|EMBL:KAB4258575.1};
OS Bacteroides uniformis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=820 {ECO:0000313|EMBL:CUP91434.1, ECO:0000313|Proteomes:UP000095788};
RN [1] {ECO:0000313|EMBL:CUP91434.1, ECO:0000313|Proteomes:UP000095788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5834942 {ECO:0000313|EMBL:CUP91434.1,
RC ECO:0000313|Proteomes:UP000095788};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RGJ93926.1, ECO:0000313|Proteomes:UP000260844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM04-30 {ECO:0000313|EMBL:RGJ93926.1,
RC ECO:0000313|Proteomes:UP000260844};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000431575, ECO:0000313|Proteomes:UP000487989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A3 {ECO:0000313|EMBL:KAB4258575.1,
RC ECO:0000313|Proteomes:UP000487989}, and BIOML-A6
RC {ECO:0000313|EMBL:KAB4242228.1, ECO:0000313|Proteomes:UP000431575};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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}.
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DR EMBL; CZBF01000003; CUP91434.1; -; Genomic_DNA.
DR EMBL; WCTM01000006; KAB4242228.1; -; Genomic_DNA.
DR EMBL; WCTJ01000002; KAB4258575.1; -; Genomic_DNA.
DR EMBL; QSPV01000006; RGJ93926.1; -; Genomic_DNA.
DR RefSeq; WP_057281688.1; NZ_WCTQ01000003.1.
DR AlphaFoldDB; A0A174S0H9; -.
DR Proteomes; UP000095788; Unassembled WGS sequence.
DR Proteomes; UP000260844; Unassembled WGS sequence.
DR Proteomes; UP000431575; Unassembled WGS sequence.
DR Proteomes; UP000487989; 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 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..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 97353 MW; 5390DCD9656999E0 CRC64;
MNFNNFTIKA QEAVQEAVNL VQSRGQQAIE PVHVLQSVMK VGENVTNFIF QKLGMNGQQI
ALVLDKQIDS LPKVSGGEPY LSRETNEVFQ KATQYSKEMG DEFVSLEPVL LALLNVKSTA
STILKDAGMT ERELREAINE LRKGEKVTSQ SSEDTYQSLE KYAINLNEAA RSGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP ILIGEPGTGK TAIVEGLAHR ILRGDVPENL KNKQVYSLDM
GALVAGAKYK GEFEERLKAV INEVKKSEGD IILFIDEIHT LVGAGKGEGA MDAANILKPA
LARGELRSIG ATTLDEYQKY FEKDKALERR FQIVMVNEPD TLSTISILRG LKERYENHHH
VRIKDDAIIA AVELSNRYIT DRFLPDKAID LMDEAAAKLR MEVDSVPEEL DEISRKIKQL
EIEREAIKRE NDKPKLEQIG KELAELKEQE NSYKAKWQSE KTLVNKIQQN KVEIENLKFE
ADKAEREGDY GRVAEIRYGK LQALNQEIEE TQQKLHEMQG DKAMIKEEVD AEDIADVVSR
WTGIPVSKML QSEKDKLLHL EAELHQRVIG QDEAIEAVSD AVRRSRAGLQ DPKRPIGSFL
FLGTTGVGKT ELAKALAEFL FDDETMMTRI DMSEYQEKHS VSRLVGAPPG YVGYDEGGQL
TEAVRRKPYS VVLFDEIEKA HPDVFNILLQ VLDDGRLTDN KGRTVNFKNT IIIMTSNMGS
GYIQSQMEKL NSSNKEQIVE ETKKEVMNML KKTIRPEFLN RIDETIMFLP LTEPEIKQIV
VLQIKSVQKM LSGNGVELVL TNAAIDFLAN AGYDPEFGAR PVKRAIQHYL LNDLSKKLLS
QEVDRSKPIT VDASTTDDGL VFRN
//
