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Database: UniProt
Entry: A0A4V2ZG89_9ALTE
LinkDB: A0A4V2ZG89_9ALTE
Original site: A0A4V2ZG89_9ALTE 
ID   A0A4V2ZG89_9ALTE        Unreviewed;       856 AA.
AC   A0A4V2ZG89;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, entry version 14.
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:TDF38646.1};
GN   ORFNames=EYS14_13390 {ECO:0000313|EMBL:TDF38646.1};
OS   Alteromonadaceae bacterium M269.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae.
OX   NCBI_TaxID=2546219 {ECO:0000313|EMBL:TDF38646.1, ECO:0000313|Proteomes:UP000295324};
RN   [1] {ECO:0000313|EMBL:TDF38646.1, ECO:0000313|Proteomes:UP000295324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M269 {ECO:0000313|EMBL:TDF38646.1,
RC   ECO:0000313|Proteomes:UP000295324};
RA   Meng X.;
RT   "Draft genome sequence of Alteromonadaceae gen. novel.";
RL   Submitted (MAR-2019) 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:TDF38646.1}.
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DR   EMBL; SMNZ01000003; TDF38646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4V2ZG89; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000295324; 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:UP000295324};
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;  95721 MW;  8B0ED5E8A5F12E67 CRC64;
     MRLDRMTSKF QIAISDAQSL ALGRDHQYIE PVHLMMSLLN QEGGSLRPLL DGVGINVNSL
     RSGLSEAIER LPKVEGVGGD VQLSKDTIIL LNLSDKISQK RKDDFITSEI FVLAATEDKG
     RLGDILRQLG VTPKKIEKAI EKMRDGQKVT DRNAEDMRQA LEKFTSDLTE RAEQGKLDPV
     IGRDDEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIVNGEVPE GLKDKRVLSL
     DMGALVAGAK YRGEFEERLK AVLSELSKEE GRIILFIDEL HTMVGAGKGE GAMDAGNMLK
     PALSRGELHC VGATTLDEYR QYIEKDAALE RRFQKVIVDQ PSVEDTIAIL RGLKERYELH
     HSVDITDPAI VAAASLSHRY ISDRQLPDKA IDLIDEAASS IRLQMDSKPE EMDRLERRII
     QLKLEERALA KETDEASHKR LELIELEREK LEFEFSDLEK VWNSEKTAVQ GTQQVKSQLE
     QAKLDLEIAR RASDLSRMSE LQYGRIPELE LKLDLAAEAE EQKFNLLKNK VTENEIADVL
     SRWTGIPVNK MLEGERDKLL RMEQVLHQQV VGQTEAVSAV SNAIRRTRAG LADPNRPIGS
     FLLLGPTGVG KTELCKSLAG FLFDTQDAIV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
     YLTEAVRRKP YSVVLLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTIDFK NTVVIMTSNL
     GSDVIQDMHT EVQYEEMKAK VLSVVSNYFR PEFINRIDDS VVFHPLGREQ IKAIAKIQLD
     KLSARLSDKH IKLSLTEAAF DKLSEAGFDP VYGARPLRRA IQTYIENPLA NKILSGEVMP
     ETTVSVDAKE GELTFN
//
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