ID W7TTU9_9STRA Unreviewed; 1000 AA.
AC W7TTU9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Atp-dependent chaperone {ECO:0000313|EMBL:EWM24016.1};
GN ORFNames=Naga_100040g42 {ECO:0000313|EMBL:EWM24016.1};
OS Nannochloropsis gaditana.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM24016.1, ECO:0000313|Proteomes:UP000019335};
RN [1] {ECO:0000313|EMBL:EWM24016.1, ECO:0000313|Proteomes:UP000019335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-31 {ECO:0000313|EMBL:EWM24016.1,
RC ECO:0000313|Proteomes:UP000019335};
RX PubMed=23966634; DOI=10.1093/mp/sst120;
RA Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT Nannochloropsis gaditana in Nitrogen Depletion.";
RL Mol. Plant 7:323-335(2014).
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:EWM24016.1}.
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DR EMBL; AZIL01001410; EWM24016.1; -; Genomic_DNA.
DR AlphaFoldDB; W7TTU9; -.
DR EnsemblProtists; EWM24016; EWM24016; Naga_100040g42.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000019335; Chromosome 15.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000019335};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1000
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004901237"
FT DOMAIN 100..244
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 977..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 510..625
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1000 AA; 110551 MW; A954549D2B9A2BD0 CRC64;
MAIKSRGRRI NFLPTACTTT LLVAACTSQS AQAFLLPFQG SRFTAPTSKA IAPASRFQSG
VSTYGLSGLL SSTDVRMDIR SRSRGSTTMM STKNNNQMSA ESYTEKAWDV ITRLPQLATR
LECQFIDNEI LLKSLLEEGP QALANRVFFK AGVKLSQLET ELDNYIASQP KVPDASNKMM
SNTLQKVLDE AFKERDAMRD QYVSVEHLLL GLVAHDSRFL KPALTKQGVT EAQIREAIAS
IRGNNVVTSR TPEASYEALE QYSRDLTQAA KDGKLDPVIG RDDEIRRTIQ ILSRRTKNNP
ILLGEPGVGK TAIAEGLAQR IVSGDVPEPL KKRRLVALDM GALIAGAKYR GEFEERLKAV
LKEVTESNGQ IIMFIDEIHT VVGAGATSGA MDASNLLKPM LARGELRCIG ATTLAEYKQF
IEKDKALERR FQQVMVEQPS VEDTIAILRG LKDRYEVHHG VRIRDSSLVA AAQLSHRYIS
DRFLPDKAID LVDEAAAKLN IEVTSKPQAV DEIDRKLIQL EMAKISLENE SSSPDSARRL
AKVEKEMAEL KKKQQELTAA WEFERKGVVV IQELKEKIDQ VKVQIEAAER EYDLGKAAQL
KYGELAKLET ELHQAEAEVE KQAAAAVGGG GESKRMLRDT VTVDDISGIV AKWTGIPVSK
LLESERDKLL GLEDELHKQV VGQDDAVRAV AEAIQRSRAG LSDPNRPIAS LVFLGPTGVG
KTLLAKKLAG YMFDDENAMI RIDMSEMMES HSLSKLIGSP PGYVGYDEGG QLTNAVRRRP
YSVILFDEME KAHPTIFNVM LQLLDDGILT DAQGNTVNFK NSIIIFTSNI GSDAILSLGG
DPEKDAEMKE VVFQAMKEQF RPEFLNRVDE FVIFSSLRKD QMKSVVRLEL LRMESRLAER
NIKVEVTDAA MDWIAEVGYD PQFGARPLKR AIQREVENVI AKGILRGEFA PNSCIFIDSN
PIEGLKILSR ELTSEVEKAG EGRVGKSDNA PADEPKLVSA
//