GenomeNet

Database: UniProt
Entry: A0A075NXM2_9ALTE
LinkDB: A0A075NXM2_9ALTE
Original site: A0A075NXM2_9ALTE 
ID   A0A075NXM2_9ALTE        Unreviewed;       858 AA.
AC   A0A075NXM2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=EP13_12445 {ECO:0000313|EMBL:AIF99424.1};
OS   Alteromonas australica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=589873 {ECO:0000313|EMBL:AIF99424.1, ECO:0000313|Proteomes:UP000056090};
RN   [1] {ECO:0000313|EMBL:AIF99424.1, ECO:0000313|Proteomes:UP000056090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 17 {ECO:0000313|EMBL:AIF99424.1,
RC   ECO:0000313|Proteomes:UP000056090};
RA   Gonzaga A., Lopez-Perez M., Rodriguez-Valera F.;
RT   "Genomes of Alteromonas australica, a world apart.";
RL   Submitted (JUN-2014) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP008849; AIF99424.1; -; Genomic_DNA.
DR   RefSeq; WP_044057518.1; NZ_DGLQ01000013.1.
DR   AlphaFoldDB; A0A075NXM2; -.
DR   GeneID; 78255711; -.
DR   KEGG; aal:EP13_12445; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000056090; Chromosome.
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:UP000056090};
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          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   858 AA;  95530 MW;  DC1FF49622F3C463 CRC64;
     MRLDRFTSKF QLAISDAQSL ALGRDHQYIE PVHLMSAMLN QQGGSVRPVL DQAKVNVNAL
     RSALSEAIER LPRVEGIGGD IQLSKESGIL LNLCDKITQQ RKDDYITSEI FVLAALQDNG
     KLGQILKQLN ITQKAIETAI DEMRGGQKVT DPNAEDVRQA LEKYTTDLTE RAEQGKLDPV
     IGRDEEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKNKRVLSL
     DMGALVAGAK YRGEFEERLK AVLNELAKEE GRVILFVDEL HTMVGAGKGD GAMDAGNMLK
     PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVEE PSVEDTIAIL RGLKERYELH
     HSVDITDPAI VAAASLSHRY ISDRQLPDKA IDLIDEAASS IRLQIDSKPE DMDRLERRII
     QLKLEEQALA KETDDASHKR LEMIELEREQ AETKYGELEK VWLKEKEAMQ GTQTIKSELE
     QAKLDLEIAR RASDLNRMSE LQYGRIPELE AKLERASEGE TVETQLVKNK VTDVEIADVL
     SRWTGIPVSK MLEGERDKLL KMEDVLHKRV VGQSEAVQSV SNAIRRSRAG LADPNRPIGS
     FLFLGPTGVG KTELCKALAG FMFDTEDAMI RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFK NTVVIMTSNL
     GSDVIQDKHN ESQYDEMKNA VMGVVGQHFR PEFINRVDDI VVFHPLGKDQ IKSIAKIQLA
     SLRARLADKG YKLTLSGAAM DKLAEAGFDP VFGARPLKRA IQVHIENPLA QQLLAGHLLP
     ESTIRIDVDG DELTVLNQ
//
DBGET integrated database retrieval system