ID C2BIL7_9FIRM Unreviewed; 858 AA.
AC C2BIL7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:EEI85269.1};
GN ORFNames=HMPREF0072_2187 {ECO:0000313|EMBL:EEI85269.1};
OS Anaerococcus lactolyticus ATCC 51172.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525254 {ECO:0000313|EMBL:EEI85269.1, ECO:0000313|Proteomes:UP000005984};
RN [1] {ECO:0000313|EMBL:EEI85269.1, ECO:0000313|Proteomes:UP000005984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51172 {ECO:0000313|EMBL:EEI85269.1,
RC ECO:0000313|Proteomes:UP000005984};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (OCT-2008) 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:EEI85269.1}.
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DR EMBL; ABYO01000283; EEI85269.1; -; Genomic_DNA.
DR RefSeq; WP_004828878.1; NZ_GG666047.1.
DR AlphaFoldDB; C2BIL7; -.
DR STRING; 525254.HMPREF0072_2187; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR Proteomes; UP000005984; 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:UP000005984};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 411..438
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 471..525
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 97170 MW; D538B3D53123FAFB CRC64;
MDNNKLTQKS IEAINNANSM AIKDANPEVN EFHLALSLVD SPSSYVSMVL SKMGVDVNAY
KKKIEDKIEN LPKQSGNANT YPSQVFQRIF LKAEDEADAM GDSFVSVEHI FLSLLKENTE
MSPINKEFNI SYKVFKDYVL KVRNGQKVTT DNPEETSNPL EKFGRDLTQE ARDGKIDPVI
GRDAEIRNAL RILSRRKKNN PVLIGQPGVG KTAIVEGLAQ RIVNNDVPEP LQGRRIFSLD
MGALVAGAKY RGQFEERLKA VIEEVKKSDG QIIMFIDEIH TIVGAGKSEG AMDASNIMKP
MLARGEIKVI GATTLNEYRE YIEKDGALER RFQKVMVEEP SVEDTISILR GIKEKYEIFH
GIRIQDSAVI AAAELSDRYI SDRFLPDKAI DLMDEACATV RTEIDTMPAY LDEQKRKLLQ
LQIEITALKK EEDDYSKKRL ADLEKELADL SDTFNEDFLK WKEQKSAIDD VKSIKEEIDK
VKVEIDQAER NYDFEKLSEL KYGKLAELEN KLKEASSTNN DESSIKEEVT DEDVADVVSS
WTNIPVSKLV ETERTKILHL GETLHERVIG QDEAIKAVSD AIIRARSGLK EQNRPIGSFI
FLGPTGVGKT ELAKTLTEAM FDDEHNMIRI DMSEYMEKYS VSRLIGAAPG YVGYEEGGQL
TEAVRRKPYS VILFDEIEKA HPDVFNILLQ VLDDGRLTDS QGRTVDFKNT IIIMTSNIGS
EFLIDGLNKD GTIKEENQKK VDEVLRRSFK PEFLNRIDDI VMFTPLTSDQ VYKIIDLQID
NIRKRLADRD IKLEITPEAK EYILANSYDV EYGARPVKRY LQRNVETKLG KLIIEGKVAD
RDTAILDLVD NQLEFKTK
//
