ID H8MPF0_CORCM Unreviewed; 874 AA.
AC H8MPF0;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:AFE08361.1};
GN OrderedLocusNames=COCOR_02397 {ECO:0000313|EMBL:AFE08361.1};
OS Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 / M2)
OS (Myxococcus coralloides).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Corallococcus.
OX NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE08361.1, ECO:0000313|Proteomes:UP000007587};
RN [1] {ECO:0000313|EMBL:AFE08361.1, ECO:0000313|Proteomes:UP000007587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC {ECO:0000313|Proteomes:UP000007587};
RX PubMed=22582372; DOI=10.1128/JB.00397-12;
RA Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W.,
RA Sogaard-Andersen L.;
RT "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus
RT coralloides DSM 2259.";
RL J. Bacteriol. 194:3012-3013(2012).
RN [2] {ECO:0000313|Proteomes:UP000007587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC {ECO:0000313|Proteomes:UP000007587};
RA Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., Sogaard-Andersen L.;
RT "Genome sequence of the fruiting myxobacterium Corallococcus coralloides
RT DSM 2259.";
RL Submitted (MAR-2012) 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; CP003389; AFE08361.1; -; Genomic_DNA.
DR RefSeq; WP_014395226.1; NC_017030.1.
DR AlphaFoldDB; H8MPF0; -.
DR STRING; 1144275.COCOR_02397; -.
DR KEGG; ccx:COCOR_02397; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_7; -.
DR InParanoid; H8MPF0; -.
DR OMA; GPEHILM; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000007587; Chromosome.
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:UP000007587};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 83..110
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 411..539
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 874 AA; 97022 MW; 216610B8EBA839AB CRC64;
MRLDKYTVKA QEAIQEGQSL ARRADNPHYE PEHLAAALLG QKDGIVDPLL RKIGVDVKLF
AGRLGEALQK LPRIQGGESA ILSQRLMKTF DKAEDEAKAL KDEFTSSEHL LLALTQDKGA
VGEAMKSSGV TRERVQAGLK EVRGSSRVTS ADAESTYQAL EKYGRDLTEA ARSGKLDPVI
GRDEEIRRCI QVLSRRTKNN PVLIGEPGVG KTAIAEGLAR RIVDGDVPEG LKNKRLITLD
LGAMVAGAKY RGEFEERLKA VLKEVADAAG EIILFIDEMH TLVGAGKAEG AMDAGNMLKP
ALARGELHCI GATTLDEYRK HIEKDAALER RFQPVFVGEP TVHDTISILR GLKERYEVHH
GVRIQDSALV AAATLSHRYI SDRFLPDKAI DLVDEASSRL RIEIDSMPTE IDDIRRKVTQ
LEIEREGLRK ETDPHSRERL STIEKELANL NEKFNSLKAH WDEEKKAIAA LRSLKEKQEK
ARNDQAAAER QGDLNRAAEL KFGVIPSLEK EVAAQNEKLA ELQKNQKFLK EEVDSEDIAS
VVAKWTGIPV SKLMEGEMQK LVKMEDRLAE RVIGQRSPIE AVSNAVRRAR SGLQDPNRPI
GSFIFLGPTG VGKTETAKAL AEFLFDDDTA MVRIDMSEYM EKHAVSRLVG APPGYVGYEE
GGQLTEAVRR RPYTVVLFDE IEKAHHDVFN ILLQILDEGR VTDSQGRTVD FRNTVLILTS
NIGSQAIQEG MAGTDTLNEK TRGEVMEALR AHFRPEFLNR VDEIVIFEPL RKKDIYRIVD
IQLGKLQKLL QAKRLTLDLT DSARELLAER GYDPTYGARP LKRAVQKYLL DPLAIKVLNG
EFAPGEHIQA DAGPDGLTFA KVLVDNSKGV KQAG
//