ID E0NV99_9BACT Unreviewed; 862 AA.
AC E0NV99;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:EFM00833.1};
GN ORFNames=HMPREF0658_2104 {ECO:0000313|EMBL:EFM00833.1};
OS Hoylesella marshii DSM 16973 = JCM 13450.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=862515 {ECO:0000313|EMBL:EFM00833.1, ECO:0000313|Proteomes:UP000004394};
RN [1] {ECO:0000313|EMBL:EFM00833.1, ECO:0000313|Proteomes:UP000004394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16973 {ECO:0000313|EMBL:EFM00833.1,
RC ECO:0000313|Proteomes:UP000004394};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-2010) 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:EFM00833.1}.
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DR EMBL; AEEI01000061; EFM00833.1; -; Genomic_DNA.
DR RefSeq; WP_006950457.1; NZ_GL397214.1.
DR AlphaFoldDB; E0NV99; -.
DR STRING; 862515.HMPREF0658_2104; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_10; -.
DR Proteomes; UP000004394; 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:UP000004394};
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..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 97026 MW; F10ECEB2C0BD5F05 CRC64;
MNFDKYTIKA QEAVQEAVNT AQRAGQQSIE PVHLLKALLT KASDVTHYIF QKLGVNGAQI
STLADSEVQH LPRVQGGQPY LSNDTNSVLL KAEDISKEMG DEFVSIESLL LALLAMRSAA
SSILKDAGCT EKEMRAAISE LRQGQKVTSQ SADENYQSLA KYAKNLVEEA RAGKLDPVIG
RDDEIRRVLQ ILSRRTKNNP ILIGEPGTGK TAIVEGLAER IVRGDVPENL KDKQLYSLDM
GALVAGAKYK GEFEERLKSV ISEVTKSEGR IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRSIG ATTLNEYQKY FEKDKALERR FQTVMVDEPD EMSAISILRG LKERYENHHK
VRIQDDACIA AVKLSERYIS DRFLPDKAID LMDEAAAKLR MERDSVPEEL DEITRKLKQL
EIEREAIKRE DDQPKIAQLD KDIADLREQE KTFRAKWESE KTLVNRIQQD KQQIENLKFE
ADRAEREGNY ERVAEIRYSK LKELQDDIEN IQLQLKATQG GEGMVREEVT EEDIAEVVSR
WTGIPVTRMM QSEREKLLHL EEELHRRVIG QDEAIAAVSD AVRRSRAGLQ DPKRPLASFI
FLGTTGVGKT ELAKALADYL FNDETMMTRI DMSEYQEKFS VSRLIGAPPG YVGYDEGGQL
TEAVRRKPYS VVLFDEIEKA HPDVFNILLQ VLDDGRLTDN KGRTVNFKNT IIIMTSNLGS
QYIQSQFEKM NNSNRDHLID ETKTTVMSML KKTIRPEFLN RIDETIMFLP LSKSEIAEVV
KLQIAAVKKM LAPQGFTLDV TPAAIDYLAT VGFDPEFGAR PVKRAIQRYV LNDLSKQILA
EKVTRDKPIV VDSFGDGLVF KN
//
