ID A0A1G4G7Q8_9BACT Unreviewed; 862 AA.
AC A0A1G4G7Q8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:SCM58323.1};
GN ORFNames=ING2E5A_1759 {ECO:0000313|EMBL:SCM58323.1};
OS Petrimonas mucosa.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Petrimonas.
OX NCBI_TaxID=1642646 {ECO:0000313|EMBL:SCM58323.1, ECO:0000313|Proteomes:UP000178485};
RN [1] {ECO:0000313|EMBL:SCM58323.1, ECO:0000313|Proteomes:UP000178485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ING2-E5A {ECO:0000313|EMBL:SCM58323.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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; LT608328; SCM58323.1; -; Genomic_DNA.
DR RefSeq; WP_071137025.1; NZ_LT608328.1.
DR AlphaFoldDB; A0A1G4G7Q8; -.
DR STRING; 1642646.ING2E5A_1759; -.
DR KEGG; pmuc:ING2E5A_1759; -.
DR Proteomes; UP000178485; Chromosome i.
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:UP000178485};
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 410..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 97522 MW; 0128A6026587082B CRC64;
MNFNNFTIKS QEAVQKAIEL AQANNQQMIE PAHLLKAVML VGENVTGFLF QKLGVNVRNL
ETALNREIES YPRVSGGDPM LSRETNAVFQ HSVDVANRMG DQFVALEHLL LAMISEKNGA
SQLMKNAGIS QNGLETAIRE LRKGEKVTSP SAEDTYQSLG KYAVNLNDRA RNGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP ILIGEPGTGK TAIAEGIAHR IVRGDVPENL KSKEIYSLDM
GALIAGAKYK GEFEERLKSV VNEVVKADGE VILFIDEIHT LVGAGKSEGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQTVMVDEPS EPDSISILRG LKERYENHHK
VRIKDEAIIA AVQLSHRYIT DRFLPDKAID LMDEAAAKLR MEVDSVPYEL DEIMRRIKQL
EIEREAIRRE NDTAKEEMLT RQIENLREEE SVLKARWQSE KELINRIQQN KIDIEDAKFQ
AEKAEREGDY GKVAELRYGK IKEKEAEIEE LKNRLHETQG DSAMIKEEVD AEDIAGVVSR
WTGIPVTRML QSEREKLLHL EEELHKRVVG QEEAITAVAD AVRRNRAGLN DPKRPIGSFI
FLGTTGVGKT ELAKALADYL FDDENMMTRI DMSEYQEKFS ATRLIGAPPG YVGYDEGGQL
TEAIRRKPYS VVLFDEIEKA HPDVFNILLQ VLDDGRLTDN KGRVVNFKNT IIIMTSNMGS
ALIRENFEKL TERNREEVVE NTRNLVLSML KQTIRPEFLN RIDDIIMFAP LKQEEIKQIV
RIQLDGVKKM LAGNSITLEY TDEAVESIAE AGYDPEFGAR PVKRVIQRKV LNQLSKDILS
GKVDNSRPIV IDAIDENVYF RN
//