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Database: UniProt
Entry: A0A1H7FUI3_9GAMM
LinkDB: A0A1H7FUI3_9GAMM
Original site: A0A1H7FUI3_9GAMM 
ID   A0A1H7FUI3_9GAMM        Unreviewed;       862 AA.
AC   A0A1H7FUI3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05216262_1013 {ECO:0000313|EMBL:SEK29619.1};
OS   Colwellia chukchiensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=641665 {ECO:0000313|EMBL:SEK29619.1, ECO:0000313|Proteomes:UP000199297};
RN   [1] {ECO:0000313|Proteomes:UP000199297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9127 {ECO:0000313|Proteomes:UP000199297};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FOBI01000001; SEK29619.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7FUI3; -.
DR   STRING; 641665.GCA_002104455_00699; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199297; 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:SEK29619.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEK29619.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199297};
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   862 AA;  95110 MW;  F8169B913875B1A1 CRC64;
     MRLERFTQTF QVAISDAQSI ALGKDHQFIE PVHLMLALLN QNASSINSLL KSAGINLAAL
     RSQVEAAIAE LAQVSGTGGE VQLSSASANI LNLCDKLAQQ QGDKYISSEI FILAALQDKG
     KLGQILKALG ASEQRVQDAI AHIRGGKNVD DANAEETRQA LEKYTVDLTE RAEQGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGHPGV GKTAIVEGLA QRIVDHEVPE GIRNKRVLSL
     DLGALVAGAK YRGEFEERLK AVLNELSQLE GQVILFIDEL HTMVGAGKTD GAMDAGNMLK
     PALARGDLHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PSVDDTIAIL RGLKERYELH
     HNVEITDPAI VAAAALSHRY VSDRQLPDKA IDLIDEAASS IRMQMDSKPE NLDRIERRLI
     QLKLEQRALS KDSDAASKKR LELISDEIES CQASYDELEE VWKTEKAAIH GTQAIKTDLE
     QARIELEAAR RAGDLNTMAE LQYSRIPNLE KQLDLASQAE MQEMTLLRNK VTDVEIADVL
     SRATGIPVSK MLEGESDKLL HMEDNLHKRV VGQSEAVVSV SNAIRRSRAG LADPDKPIGS
     FLFLGPTGVG KTELSKALAH FLFDSEEALV RVDMSEFMEK HAVARLVGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEIE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFK NTVIIMTSNI
     GSDIIQEYGD NSQYQAMKTS VIAELSRHFK PEFLNRVDET VVFHPLLAEQ IKSIADIQIS
     ALIKRLEERD ITMKLSEEAL SFVAAAGFDP IFGARPLKRS IQQEIENPLA QKLLANEFSA
     GAHIDVDFND DHLTFTASAC DG
//
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