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Database: UniProt
Entry: A0A1E7Z7U2_9ALTE
LinkDB: A0A1E7Z7U2_9ALTE
Original site: A0A1E7Z7U2_9ALTE 
ID   A0A1E7Z7U2_9ALTE        Unreviewed;       856 AA.
AC   A0A1E7Z7U2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BFC18_17845 {ECO:0000313|EMBL:OFC69580.1};
OS   Alteromonas confluentis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1656094 {ECO:0000313|EMBL:OFC69580.1, ECO:0000313|Proteomes:UP000175691};
RN   [1] {ECO:0000313|EMBL:OFC69580.1, ECO:0000313|Proteomes:UP000175691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42603 {ECO:0000313|EMBL:OFC69580.1,
RC   ECO:0000313|Proteomes:UP000175691};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) 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:OFC69580.1}.
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DR   EMBL; MDHN01000039; OFC69580.1; -; Genomic_DNA.
DR   RefSeq; WP_070126722.1; NZ_MDHN01000039.1.
DR   AlphaFoldDB; A0A1E7Z7U2; -.
DR   STRING; 1656094.BFC18_17845; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000175691; 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:UP000175691};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          405..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   856 AA;  95763 MW;  67B1C63CEA10506F CRC64;
     MRLDRFTSKF QLAISDAQSL ALGRDHQFIE PVHLMTAMLN QQGGSVRPLL DQAHVNVNAL
     RSSLAEAIER LPRVEGIGGD VQLSKESGIL LNLCDKIAQQ RKDEYITSEI FVLAALDDKG
     KLGELLRSLN ITRDQLESAI DKMRGGQKVT DPNAEDVRQA LEKYTTDLTE RAEQGKLDPV
     IGRDDEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKDKRVLSL
     DMGALVAGAK YRGEFEERLK AVLNELAKEE GRVILFIDEL HTMVGAGKGE GAMDAGNMLK
     PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PSVEDTIAIL RGLKERYELH
     HSVDITDPAI VAAATLSHRY ISDRQLPDKA IDLIDEAASS IRLQIDSKPE EMDRLERRII
     QLKLEEQALA KETDDASHKR LEMIELEREQ AETKFGDLDK IWREEKDAMQ GTQSIKTELE
     QAKLDLEIAR RASDLNRMSE LQYGRIPELE MKLEKAAENE TRETLLLKNK VTDVEIADVL
     SRWTGIPVAK MLEGERDKLL RMEDVLHTRI VGQTEAVSAV SNAIRRSRAG LADPNRPIGS
     FLFLGPTGVG KTELSKALAG FLFDTEEALV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFK NTVVIMTSNL
     GSDVIQDTHD DSQYDEMKQR VMGVVSQHFR PEFINRVDDL VVFHPLGKEQ IKSIAKIQLA
     SLRQRLIEKG YKLELSGAAM DKLADAGFDP VYGARPLKRA IQTQIENPLA QQLLSGVLMP
     ESTIRIEVRD DELIIV
//
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