ID A0A2N4X791_9BACT Unreviewed; 872 AA.
AC A0A2N4X791;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PLK42296.1};
GN ORFNames=C0V77_21490 {ECO:0000313|EMBL:PLK42296.1};
OS Emticicia sp. TH156.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Emticicia.
OX NCBI_TaxID=2067454 {ECO:0000313|EMBL:PLK42296.1, ECO:0000313|Proteomes:UP000234203};
RN [1] {ECO:0000313|EMBL:PLK42296.1, ECO:0000313|Proteomes:UP000234203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH156 {ECO:0000313|EMBL:PLK42296.1,
RC ECO:0000313|Proteomes:UP000234203};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-2017) 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:PLK42296.1}.
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DR EMBL; PKRS01000015; PLK42296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4X791; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000234203; 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:UP000234203};
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 398..523
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 97514 MW; 5E93E55B66CD3687 CRC64;
MNFNQYTIKA QEVIQKAVQI AQGNMQQAVE TGHLLKAILE EDAGTSSFML NKLNVNQQLL
VSRLEAIVNG YPKVSGAQAY LGNELSAALA KSQNYLKEFN DQFVSVELLY LGLLSGKDPV
AALMKEAGFK EKELKSTIQE LRGKNNPVKD QNAENTYQAL ARYSKNLNDL ARQGKIDPVI
GRDDEIRRVL QILSRRTKNN PILLGEPGVG KTAIVEGLAQ RIVSGDVPEN LKSKTIVSLD
MGLLIAGAKY KGEFEERLKA VIKEVTDSEG EMVLFIDEIH TLIGAGAGGE SAMDAANLLK
PALSRGELHT IGATTLAEYQ KYIEKDKALE RRFQSVMVDE PNVPDAISIL RGIKEKYELH
HGVRIQDDAV IAAVELSDRY ISDRFLPDKA IDLMDEAASK LRLEMDSMPE ELDELNRKIM
QLEIEREAIR RESNKDKESI LNKEIADLSE RRNELKAKWE NEKGSINELR SLKEQIEQLK
LEAEQAERAG DYGKVAEIRY GKLVEANNRL NQIQKDANNG QATLLNEEVS AENIAEVVAK
WTGIPVAKML QSERDKLLHL ETELHNRVAG QDEAIKVVAD AVRRSRAGLQ DPKRPIGSFL
FLGPTGVGKT ELAKALAQYL FNDDNALVRI DMSEYQERHA VSRLVGAPPG YVGYDEGGQL
TEAIRRKPYS VVLLDEIEKA HPDVWNILLQ VLDEGRLTDN KGRVANFKNT IIIMTSNMGS
NIIQEKFAEN EGWNYHLILE EAKNAVLDQL KAYVRPEFLN RIDEIVLFEP LSKLNLQKII
GIQFKQIQSR VAEQGITLEA TDEVLAKLGE EGYDPSFGAR PLKRVLQRKI LNELSKGILS
GKVHKDSVIM MELGHDGEIV FENVGNSEFE IE
//