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Database: UniProt
Entry: A0A1N6PR88_9SPIO
LinkDB: A0A1N6PR88_9SPIO
Original site: A0A1N6PR88_9SPIO 
ID   A0A1N6PR88_9SPIO        Unreviewed;       869 AA.
AC   A0A1N6PR88;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05920897_10399 {ECO:0000313|EMBL:SIQ06824.1};
OS   Alkalispirochaeta americana.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Alkalispirochaeta.
OX   NCBI_TaxID=159291 {ECO:0000313|EMBL:SIQ06824.1, ECO:0000313|Proteomes:UP000186400};
RN   [1] {ECO:0000313|EMBL:SIQ06824.1, ECO:0000313|Proteomes:UP000186400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASpG1 {ECO:0000313|EMBL:SIQ06824.1,
RC   ECO:0000313|Proteomes:UP000186400};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-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}.
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DR   EMBL; FTMS01000003; SIQ06824.1; -; Genomic_DNA.
DR   RefSeq; WP_076487966.1; NZ_FTMS01000003.1.
DR   AlphaFoldDB; A0A1N6PR88; -.
DR   STRING; 159291.SAMN05920897_10399; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000186400; 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:SIQ06824.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SIQ06824.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186400};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          412..533
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   869 AA;  97217 MW;  3866983D824FD90B CRC64;
     MNNDGMTLKA QAAVQDAAAI ANRNDHGTLE AIHLARALAA QEQGIVGAIL QRLEVPLGPF
     IRQIDEEIQK MPRVTGDHGQ LHPSPALGRI FAKAEAMPRE MGDRYVSTEH FLIAILESSD
     KAATLFTAAG VTAKAVREVL QDLRGGETVD NQDPEGKMQV LEKYCKDLTA LARQEKLDPV
     IGRDEEIRRV MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA RRIVAGDVPE SLRNKKILAL
     DLGALLAGTK FRGEFEERLK GVIEEISKSR GQIILFIDEL HTLMGAGAAE GSMDASNLLK
     PALARGELRT IGATTLDEYR KHIEKDAAFE RRFQTVYTEE PSVENAVAIL RGLKERYEVH
     HGVRILDDAL VAAATLSDRY ITNRFLPDKA IDLVDEAASR MKMEIESQPT ELDQLDRRIL
     QLDIEAQALK TETSESGRER LVKVEEEVAE LRHRRDEMHL RWKNEKDVID RIRDLKVRLE
     QLSIEETQHE REGNLAKAAE IKHGTIPQLN QEIQRLSDRL RELQSEESLL REEVTHEDIA
     RVVSSWTGIP VSKMMSSEVQ KLLQLESILE ERVVGQPRAI EAVSDAIRRN KSGIGDENRP
     TGTFLFLGPT GVGKTELAKT IASFLFDDER ALTRIDMSEY MERHAVSRLI GAPPGYVGYD
     QGGQLTEVVR RRPYSVLLFD EVEKAHPDVF NIFLQLLDEG RLTDGQGRLV DFRHTIVIMT
     SNVGSDLILA ADDLDSITDQ VQDRLRQVFK PEFLNRLDEV ITFRRLDQNH IRRIVSLELE
     RLNRRVADRG ISIEFTPQAL TRLAAIGYDP AYGARPLKRA VQQYIQNPLA KRLLGESFSQ
     GGVVLVDAVP GEGAPVRGEE AFSFALRPA
//
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