ID A0A5R9GPX5_9PROT Unreviewed; 866 AA.
AC A0A5R9GPX5;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TLS66473.1};
GN ORFNames=FEF65_09895 {ECO:0000313|EMBL:TLS66473.1};
OS Mariprofundus erugo.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=2528639 {ECO:0000313|EMBL:TLS66473.1, ECO:0000313|Proteomes:UP000306585};
RN [1] {ECO:0000313|EMBL:TLS66473.1, ECO:0000313|Proteomes:UP000306585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P3 {ECO:0000313|EMBL:TLS66473.1,
RC ECO:0000313|Proteomes:UP000306585};
RX PubMed=31076431;
RA Garrison C.E., Price K.A., Field E.K.;
RT "Environmental Evidence and Genomic Insight of Iron-oxidizing Bacteria
RT Preference Towards More Corrosion Resistant Stainless Steel at Higher
RT Salinities.";
RL Appl. Environ. Microbiol. 0:0-0(2019).
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:TLS66473.1}.
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DR EMBL; VBRY01000009; TLS66473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5R9GPX5; -.
DR OrthoDB; 5287200at2; -.
DR Proteomes; UP000306585; 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:UP000306585};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..152
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 418..505
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 96574 MW; EC4B2FF089FD615C CRC64;
MDMNRLTQKA NEALMASQSL AVRLSHQEVD GEHLLVELLA QQDGLAPRLI EQSGASLAVL
QAQLQQALAK RPRVRSSGGI EQDKVYITQR LQQLLVKAGD EASRLKDEYI SVEHLLLAFI
EEGTTTDAGR ICREQGVTRE RFLKALDAVR GHQRVTSDNP EGQYDALKKY GSDLVEMARL
GKLDPVIGRD SEIRSVIRIL SRKTKNNPVL IGEPGVGKTA IAEGLAQRIV SGDVPEGLKN
RTVFALDMMA LMAGAKYRGE FEERLKAVLK EIKEAEGKII LFIDELHTIV GAGKTEGSAD
AGNMLKPMLA RGELHCIGAT TLDEYRRYIE KDAALERRFQ PVTVDAPDVE DTISILRGLR
ERFELHHGVR IADAALVAAA TLSDRYISDR FLPDKAIDLV DEACASIRTE MDSMPAELDE
STRKVMRLEI EETALKKEKD AASLERLKGL RRELADQKER RDAMRAQWDK EKGALGEVQS
VREQIEKVRL AIEQAERNYQ LEKVAELRYG RLPELEKKLA ESEAHAAEKV LLREEVGDEE
IAGVVARWTG IPVTRLMEGE REKLLRLDTV LHERVVGQDE AVQVVADAVL RARAGIQDPK
RPIGSFLFMG PTGVGKTELA RTLARTLFDS EENMVRIDMS EYMEKHAVSR LLGAPPGYVG
FEEGGQLTEA VRRKPYCVLL FDEIEKAHAD VFNVLLQVLD DGRITDSHGR TVSFLNTIVI
MTSNIGSDYL LSGIDAHGNI SEYARNQVRT ALHAHFRPEF LNRLDDTVLF KPLSEQDVVE
ISSLFLVALK KRLASQQVTL ELSDEAARWL AREGYDPVFG ARPLKRFIQQ QVETPLARLL
IAGEAHPGSV VRVNEVDGHL AFNCES
//
