ID G7L491_MEDTR Unreviewed; 978 AA.
AC G7L491; A0A0C3W1V9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 2.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Casein lytic proteinase B3 {ECO:0000313|EMBL:AES77608.2};
DE SubName: Full=Putative ClpA/B family, P-loop containing nucleoside triphosphate hydrolase {ECO:0000313|EMBL:RHN44346.1};
GN Name=11429184 {ECO:0000313|EnsemblPlants:AES77608};
GN OrderedLocusNames=MTR_7g012820 {ECO:0000313|EMBL:AES77608.2};
GN ORFNames=MtrunA17_Chr7g0218421 {ECO:0000313|EMBL:RHN44346.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AES77608.2, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES77608.2, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES77608.2}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES77608,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:AES77608.2, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES77608,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:AES77608}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES77608};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [4] {ECO:0000313|EMBL:RHN44346.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN44346.1};
RA Pecrix Y., Gamas P., Carrere S.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CM001223; AES77608.2; -; Genomic_DNA.
DR EMBL; PSQE01000007; RHN44346.1; -; Genomic_DNA.
DR RefSeq; XP_003621390.2; XM_003621342.2.
DR AlphaFoldDB; G7L491; -.
DR STRING; 3880.G7L491; -.
DR PaxDb; 3880-AES77608; -.
DR EnsemblPlants; AES77608; AES77608; MTR_7g012820.
DR GeneID; 11429184; -.
DR Gramene; AES77608; AES77608; MTR_7g012820.
DR KEGG; mtr:11429184; -.
DR eggNOG; KOG1051; Eukaryota.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000002051; Chromosome 7.
DR Proteomes; UP000265566; Chromosome 7.
DR ExpressionAtlas; G7L491; differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; 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.
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 Hydrolase {ECO:0000313|EMBL:RHN44346.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 84..228
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 523..615
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 978 AA; 110281 MW; C61C7EC2CF183907 CRC64;
MASTTSFSLP YSTPISFNRR NSAIYFSHHH RVSLSFSAKR VSLKSSLPLN QRRFLANGIC
RTQTNSKRFS VRCEASSTGT GRITQQEFTE MAWQAIVSSP EVAKENKHQI VETEHLMKAL
LEQKNGLARR IFTKVGVDNT QLLEATDKFI QRQPKVIGES AGSMLGRDLE GLIQRARDFQ
KEYGDSFVSV EHLVLGFIQD QRFGKQLFKD FQISQQGLKS AIESIRGRQS VIDQDPEGKY
EALEKYGKDL TAMAKAGKLD PVIGRDDEIR RCIQILSRRT KNNPVLIGEP GVGKTAISEG
LAQRIVQGDV PQALMNRRLI SLDMGALIAG AKYRGEFEDR LKAVLKEVTE SDGQTILFID
EIHTVVGAGA TNGAMDAGNL LKPMLGRGEL RCIGATTLDE YRKYIEKDPA LERRFQQVYV
DQPTVEDTIS ILRGLRERYE LHHGVRISDS ALVEAAILSD RYISGRFLPD KAIDLVDEAA
AKLKMEITSK PTALDEINRS VLKLEMERLS LTNDTDKASK DRLSRLEAEL SLLKHKQAEL
TEQWEHEKSV MTRLQSIKEE IDRVNLEIQQ AEREYDLNRA AELKYGSLNS LQRQLESAEK
ELDEYMNSGK SMLREEVTGS DIAEIVSKWT GIPVSKLQQS EREKLLYLEE VLHKRVVGQD
PAVKAVAEAI QRSRAGLSDP HRPIASFMFM GPTGVGKTEL AKTLASYMFN TEEALVRIDM
SEYMEKHAVS RLIGAPPGYV GYEEGGQLTE TVRRRPYAVI LFDEIEKAHS DVFNVFLQIL
DDGRVTDSQG RTVSFTNTVI IMTSNVGSQY ILNTDDDTAP KELAYETIKQ RVMDAARSIF
RPEFMNRVDE YIVFQPLDRD QISSIVRLQL ERVQKRITDR KMKIQVTDAA IQLLGSLGYD
PNYGARPVKR VIQQNVENEL AKGILRGEFK DEDTILVDTE LTALANNQLP QQKLVFRKIE
VDSRSTPQES LEHSSQAP
//