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Database: UniProt
Entry: A0A1G6H040_9GAMM
LinkDB: A0A1G6H040_9GAMM
Original site: A0A1G6H040_9GAMM 
ID   A0A1G6H040_9GAMM        Unreviewed;       859 AA.
AC   A0A1G6H040;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05421749_101616 {ECO:0000313|EMBL:SDB87632.1};
OS   Acinetobacter marinus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=281375 {ECO:0000313|EMBL:SDB87632.1, ECO:0000313|Proteomes:UP000242317};
RN   [1] {ECO:0000313|Proteomes:UP000242317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 3699 {ECO:0000313|Proteomes:UP000242317};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-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}.
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DR   EMBL; FMYK01000001; SDB87632.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6H040; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000242317; 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:SDB87632.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDB87632.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242317};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..143
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          409..489
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   859 AA;  94711 MW;  247EF13CE6C8F343 CRC64;
     MRFEKFSDRL QQSLSDAQSL ATGKDHTSIG TIHILATLLE ESSNQSLLQQ AGVKLTELKD
     KLNQALQDAP TIANPTGDVN FNPEAAKVLN LADGYAQKAG DEFLTTDWVL LALAEQGETH
     KLFTAAGGDG KKLRSVIEKI RGNEKVTTSN HEENRDALGK YTIDLTDRAL AGKLDPVIGR
     DDEIRRTIQV LSRRTKNNPV LIGEPGVGKT AIVEGLAQRI VNGEVPESLK GKRVLSLDLG
     SLLAGAKYRG EFEERLKAVL KELAKLEGQV ILFIDEIHTL VGAGKTDGAM DAGNMLKPAL
     ARGELRCVGA TTLDEYRQYI EKDPALERRF QKVLVDEPSV EDTIAILRGL KEKYATHHGV
     QILDSAIIAA AKMSQRYITD RQLPDKAIDL IDEAASRIKM ELDSKPEALD KLDRRLIQLK
     MQFEQVKKEE DAGSKSQASL LERQINETQK EYNDLEEVWR ADKALVEGNK DVQVKLDQAK
     IALEKAQREG DLAEAGRLQY GVIPELQKQL EKAEVADENE APKLLRNKVT DNEIAEVVSA
     ATGIPVSKML QGERDKLLNM ESFLHNRVVG QDEAVKAVSN AVRRSRAGLS DPNRPSGSFL
     FLGPTGVGKT ELTKALANFL FDSDDAMIRI DMSEFMEKHS VSRLVGAPPG YVGYEEGGVL
     TEAVRRKPYS VILFDEVEKA HPDVFNILLQ VLDDGRLTDS QGRVVDFKNT VIVMTSNLGS
     QDVRELGEGA SDDDVRAVVM AAIGQHFRPE FINRIDEVVV FHGLQKSQMR GIADIQLARL
     RDRLAEREIG LRIEDDAFGL LIDAGYDPVF GARPLKRAIQ SKVENELAND ILSGKFSAGD
     TIVVSKDGDH LAFEKLKLS
//
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