ID D4H8X5_DENA2 Unreviewed; 867 AA.
AC D4H8X5;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Dacet_1710 {ECO:0000313|EMBL:ADD68474.1};
OS Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Geovibrionaceae; Denitrovibrio.
OX NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD68474.1, ECO:0000313|Proteomes:UP000002012};
RN [1] {ECO:0000313|EMBL:ADD68474.1, ECO:0000313|Proteomes:UP000002012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12809 / NBRC 114555 / N2460
RC {ECO:0000313|Proteomes:UP000002012};
RX PubMed=21304711; DOI=10.4056/sigs.892105;
RA Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT (N2460).";
RL Stand. Genomic Sci. 2:270-279(2010).
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; CP001968; ADD68474.1; -; Genomic_DNA.
DR RefSeq; WP_013010985.1; NC_013943.1.
DR AlphaFoldDB; D4H8X5; -.
DR STRING; 522772.Dacet_1710; -.
DR PaxDb; 522772-Dacet_1710; -.
DR KEGG; dap:Dacet_1710; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_0; -.
DR InParanoid; D4H8X5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000002012; 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 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:UP000002012};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 4..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 406..541
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 97448 MW; EA0753B5D9B19121 CRC64;
MFNFNKMTIK AQEAVQSALE LAEQHSHQQL MPEHLLLALM TQEEGMVTPL LQKAGVNTNQ
LITDTEKLLG KYPKVEGNVQ LYIGQEAKKA LDYAFEMIKK FGDEYVSTEH ILLGVGENAD
SNLRSALSAN GYSLNTLLKA YESVKGSTRV TDQNPEDKMN ALDKYTIDLT ESARAGKLDP
VIGRDEEIRR VIHVLSRRTK NNPVLIGEPG VGKTAIAEGL AQRIVNGDVP ETLKGRTVAA
LDMGLLIAGT KFRGEFEDRL KALLNTIKER HGEIVLFIDE MHTLVGAGKT DGAMDAANLL
KPALARGELH CIGATTLDEY KKYVEKDTAL ERRFQPVMVK EPSVEDTVSI LRGLKERYEV
HHGVRITDNA IVAAAHMANK YISDRFMPDK AIDLIDEATA KIRMEIDSLP TELDELERRI
THLEIDKQAL KKEKDNASKQ RLEKLENELA NLKEQAQSMR AAWQNEKDVI QNVRHIKEQI
EQTKHEMASA ERLGDLTKAS ELKYSKLVEL ESRLQGANSK LSELQKNKRI LKEEVDEEDI
ATVISKWTGI PATRLLEEEA DKLIRMEDYL HKRVVGQDNA IRVVSESVRR SRAGLNDPGK
PIGSFIFLGP TGVGKTELAK SLAEFLFDSE DAIVRIDMSE YMEKHSVARL IGAPPGYVGY
DEGGQLTEAV RRRPYSVILM DEIEKAHSDV FNVLLQLLDD GRLTDSKGRT VSFKNCVIIM
TSNIASDMIH DAFAEDGDWE QKYSSIQKIA ISQLSGYFRP EFLNRIDDIV VFHPLNETHI
TEIAEILMQV FAKRVLENNI ELNWTKNVIN EIVKAGFDAA YGARPMKRAI RRMVENFIAE
KIIKGELKAG DKCLLDFDGN QMILKFS
//
