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Database: UniProt
Entry: V6F8G8_MAGGM
LinkDB: V6F8G8_MAGGM
Original site: V6F8G8_MAGGM 
ID   V6F8G8_MAGGM            Unreviewed;       862 AA.
AC   V6F8G8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 65.
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:CDL00963.1};
GN   OrderedLocusNames=MGMSRv2__3748 {ECO:0000313|EMBL:CDL00963.1};
OS   Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS   / MSR-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=431944 {ECO:0000313|EMBL:CDL00963.1, ECO:0000313|Proteomes:UP000018922};
RN   [1] {ECO:0000313|EMBL:CDL00963.1, ECO:0000313|Proteomes:UP000018922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1
RC   {ECO:0000313|Proteomes:UP000018922};
RX   PubMed=24625872; DOI=10.1128/genomeA.00171-14;
RA   Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA   Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA   Wang L., Li J.;
RT   "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL   Genome Announc. 2:e00171-e00114(2014).
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. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
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|ARBA:ARBA00004496,
CC       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; HG794546; CDL00963.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6F8G8; -.
DR   STRING; 1430440.MGMSRv2__3748; -.
DR   KEGG; mgy:MGMSRv2__3748; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_5; -.
DR   Proteomes; UP000018922; Chromosome I.
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:UP000018922};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          414..494
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   862 AA;  94845 MW;  E93717034A4A6352 CRC64;
     MDFEKYSERC KGFVQAAQTL ALRYGHQRLM PEHLLKVLLD DKDGLAAKLI KAAGGDHKKA
     LAGVEAEIAK QPKVEGPGAS GLHLTGELAR VFQLAEEAAT KSGDQYVTAE RLLLALTMGA
     GTASARILSE AGVNPQALNR AIDDMRKGRK ANSASAEDGY DALKKYARDL TAAAREGKLD
     PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIIEG LAIRIVNGDV PENLKLKSLM
     SLDMGSLIAG AKFRGEFEER LKAVLSEIQA ANGDVILFID EMHTLVGAGA AEGAMDASNL
     LKPALARGEL HCVGATTLNE YRKHVEKDAA LARRFQPVFV SEPNVEDTIS ILRGIKEKYE
     MHHGVRISDS SLVAAATLSN RYITDRFLPD KAIDLVDEAA SRLRMEVDSK PEELDEIDRR
     IVQLKIEREA LKKETDPASR DRLLTLEDEL IELEADSDRI TNEWRAEKDQ LASATKLKEQ
     LDAARIEADK AQREGQYQKA GELLYGLIPD LERKLATADA AEGRMLNEAV TEEHIAGVVS
     RWTGIPVDKM LAGEREKLLD MENRLKKRVI GQDEALVAVS NAVRRARAGL QDPNRPIGSF
     LFLGPTGVGK TELTKALAEF LFDDETAMVR MDMSEYMEKH SVARLIGAPP GYVGYEEGGA
     LTEAVRRRPY QVILFDEVEK AHPDVFNVLL QVLDDGRLTD GQGRTVDFRN TLIVLTSNLG
     SDILANQEEG HDSGEVRDLV MEVVRASFRP EFLNRLDEIL LFHRLGRAHM TGIVQIQLAW
     LRHLLADRKI VLDLDDSANE WLAQKGYDPI YGARPLKRVI QRALQNPLAG LILEGRVCDG
     AKVTVSGPSG VLTINGQAVE LT
//
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