ID Q9S822_MAIZE Unreviewed; 912 AA.
AC Q9S822;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 142.
DE SubName: Full=Heat shock protein 101 {ECO:0000313|EMBL:AAD25223.1};
DE SubName: Full=Heat shock protein HSP101 {ECO:0000313|EMBL:AAD33606.1};
GN Name=HSP101 {ECO:0000313|EMBL:AAD33606.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AAD33606.1};
RN [1] {ECO:0000313|EMBL:AAD25223.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10216257; DOI=10.1016/S0378-1119(99)00060-8;
RA Nieto-Sotelo J., Kannan K.B., Martinez L.M., Segal C.;
RT "Characterization of a maize heat-shock protein 101 gene, HSP101, encoding
RT a ClpB/Hsp100 protein homologue.";
RL Gene 230:187-195(1999).
RN [2] {ECO:0000313|EMBL:AAD33606.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11706162; DOI=10.1104/pp.127.3.777;
RA Young T.E., Ling J., Geisler-Lee C.J., Tanguay R.L., Caldwell C.,
RA Gallie D.R.;
RT "Developmental and thermal regulation of the maize heat shock protein,
RT HSP101.";
RL Plant Physiol. 127:777-791(2001).
RN [3] {ECO:0000313|EMBL:AAD25223.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12119379; DOI=10.1105/tpc.010487;
RA Nieto-Sotelo J., Martinez L.M., Ponce G., Cassab G.I., Alagon A.,
RA Meeley R.B., Ribaut J.M., Yang R.;
RT "Maize HSP101 plays important roles in both induced and basal
RT thermotolerance and primary root growth.";
RL Plant Cell 14:1621-1633(2002).
RN [4] {ECO:0000313|EMBL:AAD25223.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15703059; DOI=10.1111/j.1365-313X.2005.02333.x;
RA Dinkova T.D., Zepeda H., Martinez-Salas E., Martinez L.M., Nieto-Sotelo J.,
RA de Jimenez E.S.;
RT "Cap-independent translation of maize Hsp101.";
RL Plant J. 41:722-731(2005).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; AF077337; AAD25223.1; -; Genomic_DNA.
DR EMBL; AF133840; AAD33606.1; -; mRNA.
DR RefSeq; NP_001104935.1; NM_001111465.1.
DR AlphaFoldDB; Q9S822; -.
DR SMR; Q9S822; -.
DR GeneID; 541780; -.
DR KEGG; zma:541780; -.
DR OrthoDB; 35211at2759; -.
DR ExpressionAtlas; Q9S822; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; 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 PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF190; CLP R DOMAIN-CONTAINING PROTEIN; 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:AAD33606.1}.
FT DOMAIN 3..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 408..502
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 912 AA; 101132 MW; 13F1EAA4BEA610E2 CRC64;
MNPDNFTHKT NEAIVGAHEI AVEAGHAQLT PLHLAAVLAA DKGGILRQAI TGASGGDGAA
GDSFERVLNN SLKKLPSQSP PPDSVPASTA LIKVIRRAQS AQKKRGDSHL AVDQLLLGLL
EDSQISDCLK EAGVSAARVR AELEKLRGGE GRRVESASGD TNFQALKTYG RDLVEQAGKL
DPVIGRDEEI RRVVRILSRR TKNNPVLIGE PGVGKTAVVE GLAQRIVRGD VPSNLLDVRL
IALDMGALVA GAKYRGEFEE RLKAVLKEVE EAEGKVILFI DEIHLVLGAG RTEGSMDAAN
LFKPMLARGQ LRCIGATTLE EYRKYVEKDA AFERRFQQVF VAEPSVPDTV SILRGLKEKY
EGHHGVRIQD RALVVAAQLS ARYIMGRHLP DKAIDLVDEA CANVRVQLDS QPEEIDNLER
KRIQLEVELH ALEKEKDKAS KARLIEVRKE LDDLRDKLQP LTMKYRKEKE RIDEIRKLKQ
RREELQFTLQ EAERRMDLAR VADLKYGALQ EIDAAISKLE SETGENLMLT ETVGPEQIAE
VVSRWTGIPV TRLGQNDKER LVGLADRLHQ RVVGQTEAVS AVAEAVLRSR AGLGRPQQPT
GSFLFLGPTG VGKTELAKAL AEQLFDDENL LVRIDMSEYM EQHSVARLIG APPGYVGHEE
GGQLTEQVRR RPYSVILFDE VEKAHVAVFN TLLQVLDDGR LTDGQGRTVD FRNTVIIMTS
NLGAEHLLAG MVGKNSMKVA RDLVMQEVRR HFRPELLNRL DEIVIFDPLS HEQLRKVARL
QMKDVAVRLA ERGIALAVTD AALDIILSLS YDPVYGARPI RRWIEKRVVT QLSKMLIQEE
IDENCTVYID AAPGKDELVY RVDRSGGLVN AETGMKSDIL IQVPNSSTRS DAAQAVKKMR
IMEEDEDGMD EE
//
