ID A0A094JBV3_9GAMM Unreviewed; 857 AA.
AC A0A094JBV3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=HR45_09970 {ECO:0000313|EMBL:KFZ37345.1};
OS Shewanella mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1515746 {ECO:0000313|EMBL:KFZ37345.1, ECO:0000313|Proteomes:UP000029264};
RN [1] {ECO:0000313|EMBL:KFZ37345.1, ECO:0000313|Proteomes:UP000029264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YQH10 {ECO:0000313|EMBL:KFZ37345.1,
RC ECO:0000313|Proteomes:UP000029264};
RA Liu Y., Zeng R.;
RT "Shewanella sp. YQH10.";
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 -!- 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:KFZ37345.1}.
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DR EMBL; JPEO01000006; KFZ37345.1; -; Genomic_DNA.
DR RefSeq; WP_037442441.1; NZ_JPEO01000006.1.
DR AlphaFoldDB; A0A094JBV3; -.
DR STRING; 1515746.HR45_09970; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000029264; 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:UP000029264};
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..461
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 857 AA; 95828 MW; 9DA1108BB127F72D CRC64;
MRLDRMTNKF QIAISDAQSL ALGRDHQFIE PVHLMMALLN QDSGSIHPLL TQAGIQVSTL
RSLLTQELER LPQIEGTGGD VQLSQALIRL LNLCDKLAQK RSDKFISSEL FVLAALEGGD
VLAKCLKQAG ATKELMEKTI EQIRGGQKVD DPNAEDQRQA LKKYTVDLTE RAEQGKLDPV
IGRDDEIRRT IQVLQRRSKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GIKNKRVLSL
DMGSLVAGAK YRGEFEERLK AVLNELSQEE GQVILFIDEL HTMVGAGKSE GSMDAGNMLK
PALARGELHC VGATTLDEYR QYVEKDAALE RRFQKVLVDE PSVEDTIAIL RGLKERYELH
HHVEITDPAI VAAATMSHRY ISDRKLPDKA IDLIDEAASS IRLQIDSKPE PLDKLERRAI
QLKLEEQALV KENDEASRKR LDHLRTELDD VERKAAELNE VWFTEKAALA GTQHIKADLE
QARMDLEVAR RASDLTRMSE LQYGRIPELE KQLDLAAQAE MQDMQLLRNK VTDVEIAEVL
SKATGIPVSK MLEGEREKLL HMEDALHERV IGQSEAVDAV ANAIRRSRAG LADPNRPIGS
FLFLGPTGVG KTELCKSLAK FLFDTEGAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NAVVIMTSNL
GSDVIQEHFA TASYDEMKQQ VLNVVQMHFR PEFLNRIDET VVFHPLEAEH IKSIAAIQIE
TLRQRLAEKE YQLDISDAAL DFIAKAGFDP VYGARPLKRA LQQEVENPLA QSLLQGKLLP
GKTIHVDFRE GELTFRQ
//