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Database: UniProt
Entry: A0A1G4G7Q8_9BACT
LinkDB: A0A1G4G7Q8_9BACT
Original site: A0A1G4G7Q8_9BACT 
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
//
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