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Database: UniProt
Entry: A0A133YIL9_9BACT
LinkDB: A0A133YIL9_9BACT
Original site: A0A133YIL9_9BACT 
ID   A0A133YIL9_9BACT        Unreviewed;       863 AA.
AC   A0A133YIL9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, 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   ORFNames=HMPREF1870_01430 {ECO:0000313|EMBL:KXB43041.1};
OS   Bacteroidales bacterium KA00344.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1497954 {ECO:0000313|EMBL:KXB43041.1, ECO:0000313|Proteomes:UP000070254};
RN   [1] {ECO:0000313|Proteomes:UP000070254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00344 {ECO:0000313|Proteomes:UP000070254};
RA   Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA   O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA   Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-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}.
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:KXB43041.1}.
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DR   EMBL; LSCT01000120; KXB43041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133YIL9; -.
DR   STRING; 1497954.HMPREF1870_01430; -.
DR   PATRIC; fig|1497954.3.peg.1451; -.
DR   Proteomes; UP000070254; 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   Reference proteome {ECO:0000313|Proteomes:UP000070254};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          4..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          404..522
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   863 AA;  97953 MW;  3C7FC1E1AC9A589B CRC64;
     MMTFEKFTIK AQEAVQEAVN TAQQANQQAI EPIHLLQGII QKGKDVTNFV FQKLGINVMQ
     IENLVQNELQ HLPRVEGGQP YFSNETNQVL QRAIDLAQKM GDEFVSVEPM LLAILQSNSP
     AGRILKDAGC TEEGLKKAIQ ELRQGQKVQS QSGDENYQAL SKYAKNLVDE ARKGKLDPVI
     GRDEEIRRVL QILSRRTKNN PILIGEPGTG KTAIAEGLAQ RIVRGDVPEN LKNKQLYSLD
     MGALVAGAKY KGEFEERLKS VIKEVTSAEG NIILFIDEIH TLVGAGGGEG AMDAANILKP
     ALARGELRVI GATTLNEYQK YFEKDAALER RFQTVMVDEP SELDAISILR GLKERYENHH
     KVRIQDDACI AAVQLSERYI SDRFLPDKAI DLMDEAAAKL RMERDSVPEE LDEITRRLKQ
     LEIEREAIKR ENDEAKIQQL DKDIAELKEQ EHQYRAKWET EKGLVNKIQQ DKQEMENLRF
     EAERAEREGN YGRVAEIRYG KLKQLQDDID NIQIQLKATQ GGDAMIREEV TADDIAEVVS
     RWTGIPVTRM MQSEREKLLH LEAELHQRVI GQNEAIQAVS DAVRRSRAGL QDPKKPIASF
     IFLGTTGTGK TELAKALAEY LFNDENMMTR IDMSEYQEKF SVSRLIGAPP GYVGYDEGGQ
     LTESVRRKPY SVVLFDEIEK AHPDVFNILL QVLDDGRLTD NKGRTVNFKN TIIIMTSNLG
     SQYIQERFAD LNDHNREEVI NDTRHNVMEM LKKTIRPEFL NRIDDIIMFL PLTKHEIAEI
     VTLQMNRVRR MLEPQGFNIE WTPDAIDWLA GVGYNPEFGA RPVKRAIQEY VLNDLSKKLL
     AEKVIREKPI VVDANADGLV FRN
//
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