ID A0A2T0XAN3_9BACT Unreviewed; 861 AA.
AC A0A2T0XAN3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=DFO77_12810 {ECO:0000313|EMBL:RCW29410.1};
OS Marinilabilia salmonicolor.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Marinilabilia.
OX NCBI_TaxID=989 {ECO:0000313|EMBL:RCW29410.1, ECO:0000313|Proteomes:UP000252733};
RN [1] {ECO:0000313|EMBL:RCW29410.1, ECO:0000313|Proteomes:UP000252733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=160A {ECO:0000313|EMBL:RCW29410.1,
RC ECO:0000313|Proteomes:UP000252733};
RA Lamendella R.;
RT "Freshwater and sediment microbial communities from various areas in North
RT America, analyzing microbe dynamics in response to fracking.";
RL Submitted (JUL-2018) 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:RCW29410.1}.
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DR EMBL; QPIZ01000028; RCW29410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0XAN3; -.
DR STRING; 1168289.GCA_000259075_03310; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000252733; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:RCW29410.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RCW29410.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000252733};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..142
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 401..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 97067 MW; 9C1E47EFB08F9779 CRC64;
MNLNQFTIKA QEAIQQAFQI AGGYQHQAIE NGHLLKGLLE VEENITRFLF NKMGVGQLTP
VLDKMIESYP KVSGGDPYLS REANESLQKA VTFSKEMGDQ FASIEHMLLG ILKSGDQVSK
MMKDAGVTEK GLKQAIEELR KGSKVESQSA EDAFNALGRF AIDLNEQARS GKLDPVIGRD
DEIRRILQIL SRRTKNNPIL IGEPGVGKTA IAEGLAHRII NGDVPENLKS KRIFSLDMGA
LVAGAKYKGE FEERLKAVVK EVVGSNGEIV LFIDEIHTLV GAGKSEGAMD AANILKPALA
RGELRAIGAT TLGEYQKYFE KDKALERRFQ IVMVDEPDLA SAISILRGLK ERYETHHRVR
IKDEAIISAA ELSKRYISDR FLPDKAIDLI DEAASKLRLE MNSVPEEIDE IERRIKQLEI
EREAIRREGD KKKVNELSEE ISNLKEERNG LRARWEEEKG IIEQIQKNKE AIEQYKFEAD
RAEREGLYEK VAELRYGRIK EANETIEKLQ LQLAERQSQS AMIKEEVDAE DVAQIVSRWT
GIPVTRMLQS ERQKLLKLED QLHKRVVGQD EAIAAVADAV RRSRAGLQDV RRPIGSFIFL
GTTGVGKTEL ARALAEFLFD DEDLMTRIDM SEYQERHSVS RLIGAPPGYV GYDEGGQLTE
AVRRKPYSVV LLDEIEKAHP DVFNILLQVL DDGRLTDNKG RHADFKNTII IMTSNVGSHL
IQKNFEEAGA SGFSGEVVEK TRQEVMALLK QTIRPEFLNR IDDIITFSPL SKEEIREIVK
LQFEQISRLL KTQDVSIEMS DAAIDHLAEV GYDPLFGARP IKRALQRFVL NDLSKKLLAD
EVDKERPIRV DFKDGNLEFT N
//