ID Q9XQC7_ARATH Unreviewed; 326 AA.
AC Q9XQC7; Q9FN80;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 24-JAN-2024, entry version 174.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN Name=EMB1241 {ECO:0000313|EMBL:AED92459.1,
GN ECO:0000313|TAIR:AT5G17710};
GN Synonyms=embryo defective 1241 {ECO:0000313|EMBL:AED92459.1}, grpE
GN {ECO:0000313|EMBL:CAB40381.1}, MVA3.60 {ECO:0000313|EMBL:AED92459.1},
GN MVA3_60 {ECO:0000313|EMBL:AED92459.1};
GN OrderedLocusNames=At5g17710 {ECO:0000313|Araport:AT5G17710,
GN ECO:0000313|EMBL:AED92459.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast {ECO:0000313|EMBL:CAB40381.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:CAB40381.1};
RN [1] {ECO:0000313|EMBL:BAB09570.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [2] {ECO:0000313|EMBL:CAB40381.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Columbia {ECO:0000313|EMBL:CAB40381.1};
RA Kikuchi S., Kogata N., Nakai M.;
RT "cDNA sequence of chloroplast GrpE from Arabidopsis thaliana.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AED92459.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130714; DOI=10.1038/35048507;
RG Kazusa DNA Research Institute;
RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG European Union Arabidopsis Genome Sequencing Consortium;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D.,
RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B.,
RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H.,
RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S.,
RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J.,
RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4] {ECO:0000313|EMBL:AED92459.1}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:AED92459.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Essential component of the PAM complex, a complex required
CC for the translocation of transit peptide-containing proteins from the
CC inner membrane into the mitochondrial matrix in an ATP-dependent
CC manner. {ECO:0000256|RuleBase:RU000640}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU000640}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|RuleBase:RU004478}.
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DR EMBL; CP002688; AED92459.1; -; Genomic_DNA.
DR EMBL; AB006706; BAB09570.1; -; Genomic_DNA.
DR EMBL; AJ010819; CAB40381.1; -; mRNA.
DR RefSeq; NP_850840.1; NM_180509.4.
DR AlphaFoldDB; Q9XQC7; -.
DR SMR; Q9XQC7; -.
DR STRING; 3702.Q9XQC7; -.
DR PaxDb; 3702-AT5G17710-2; -.
DR ProMEX; Q9XQC7; -.
DR EnsemblPlants; AT5G17710.2; AT5G17710.2; AT5G17710.
DR GeneID; 831638; -.
DR Gramene; AT5G17710.2; AT5G17710.2; AT5G17710.
DR Araport; AT5G17710; -.
DR TAIR; AT5G17710; EMB1241.
DR eggNOG; KOG3003; Eukaryota.
DR OrthoDB; 36313at2759; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XQC7; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0034605; P:cellular response to heat; IGI:TAIR.
DR GO; GO:0006457; P:protein folding; IDA:TAIR.
DR GO; GO:0050821; P:protein stabilization; IGI:TAIR.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 1.
DR HAMAP; MF_01151; GrpE; 1.
DR InterPro; IPR000740; GrpE.
DR InterPro; IPR013805; GrpE_coiled_coil.
DR InterPro; IPR009012; GrpE_head.
DR PANTHER; PTHR21237; GRPE PROTEIN; 1.
DR PANTHER; PTHR21237:SF27; GRPE PROTEIN HOMOLOG; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF58014; Coiled-coil domain of nucleotide exchange factor GrpE; 1.
DR SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 1: Evidence at protein level;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU000640};
KW Chloroplast {ECO:0000313|EMBL:CAB40381.1};
KW Mitochondrion {ECO:0000256|RuleBase:RU000640};
KW Plastid {ECO:0000313|EMBL:CAB40381.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9XQC7,
KW ECO:0007829|ProteomicsDB:Q9XQC7};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT REGION 69..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..105
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 326 AA; 35721 MW; CD2397979A588817 CRC64;
MAGLLKTPSL HLTPTLLHAP SVPFKPFCVS FAGGRNVSVS LSRRASLRSV SSGYPLRLLN
LVPFASGEAE TTETEVESNE PEVQETDGAV DVENENASAE EGEAEEEEAA VITALLKSYK
EALADNNEGK IAEIEASLKS IEDEKFLLAD KVASLSNELS VERDRLIRIS ADFDNFRKRT
ERERLNLVSN AQGEVVENLL AVLDNFERAK SQIKVETEGE EKVTNSYQSI YKQFVEILGS
LGVIHVETVG KQFDPMLHEA IMREDSAEYE EGIVLEEYRK GFLLGERLLR PSMVKVSAGP
GPEKPLEAEG EEATAQGSAE EESSSS
//
