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Database: UniProt
Entry: A0A037ZPT0_9RHOB
LinkDB: A0A037ZPT0_9RHOB
Original site: A0A037ZPT0_9RHOB 
ID   A0A037ZPT0_9RHOB        Unreviewed;       871 AA.
AC   A0A037ZPT0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-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=ACMU_03340 {ECO:0000313|EMBL:KAJ57553.1};
OS   Actibacterium mucosum KCTC 23349.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Actibacterium.
OX   NCBI_TaxID=1454373 {ECO:0000313|EMBL:KAJ57553.1, ECO:0000313|Proteomes:UP000026249};
RN   [1] {ECO:0000313|EMBL:KAJ57553.1, ECO:0000313|Proteomes:UP000026249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 23349 {ECO:0000313|EMBL:KAJ57553.1,
RC   ECO:0000313|Proteomes:UP000026249};
RA   Arahal D.R., Shao Z., Lai Q., Pujalte M.J.;
RT   "Draft Genome Sequence of Actibacterium mucosum KCTC 23349, a Marine
RT   Alphaproteobacterium with Complex Ionic Requirements Isolated from
RT   Mediterranean Seawater at Malvarrosa Beach, Valencia, Spain.";
RL   Submitted (MAR-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. 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}.
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:KAJ57553.1}.
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DR   EMBL; JFKE01000001; KAJ57553.1; -; Genomic_DNA.
DR   RefSeq; WP_035255934.1; NZ_JFKE01000001.1.
DR   AlphaFoldDB; A0A037ZPT0; -.
DR   STRING; 1454373.ACMU_03340; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000026249; 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:UP000026249};
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..529
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  95317 MW;  AAD4D21E137F3ECE CRC64;
     MNMEKFTERS RGFIQAAQTI AMRESHQRLA PEHLLKALLD DDQGLAANLI KRAGGAPDRV
     VEAVDVALSK IPQVGGDAGQ TYLDQQTAKV LAEAEKVATK AGDSFVPVER ILTALAMVKS
     KAREALEAGA VSAQKLNAAI NDIRKGRTAD TASAEEGYDA LKKYARDLTE AARDGKIDPI
     IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIIDGDVPE SLRNKQLMAL
     DMGALIAGAK YRGEFEERLK SILKEIEAAA GEVILFIDEM HTLVGAGKTD GAMDAANLIK
     PALARGELHC VGATTLDEYR KHVEKDAALA RRFQPVLVDE PTVEDTISIL RGIKEKYELH
     HGVRISDSAL VAASTLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDALDRQIL
     QLQIEAEALK KEDDAASKDR LTKLEKELSE LQQQSAGLTA KWQAERDKLE SGRELKEQLD
     RARAELDAAK RDGNLAKAGE LSYGVIPELE KKLTEAEEAE NDLMVEEAVR PEQIAQVVER
     WTGIPTSKML EGEREKLLRM EDEIGKRVIG QSQAVTAVAN AVRRARAGLN DENRPLGSFL
     FLGPTGVGKT ELTKAVAEYL FDDDSAMVRI DMSEFMEKHA VARLIGAPPG YVGYDEGGVL
     TEAVRRKPYQ VVLFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRTVDFKQT LIILTSNLGS
     QALSQLPDGA DSAQARRDVM DAVRAHFRPE FLNRLDETII FDRLGRADMD GIVAIQLARL
     QKRLAGRNIT LDLDDAALKW LADEGYDPVF GARPLKRVIQ RALQDQLAEA LLGGDILDGA
     HVQVSAGADG LLVGDRVGKS LREPPNDAVV H
//
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