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Database: UniProt
Entry: F6HMV2_VITVI
LinkDB: F6HMV2_VITVI
Original site: F6HMV2_VITVI 
ID   F6HMV2_VITVI            Unreviewed;       338 AA.
AC   F6HMV2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN   OrderedLocusNames=VIT_08s0056g00810 {ECO:0000313|EMBL:CCB55977.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB55977.1, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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; FN595995; CCB55977.1; -; Genomic_DNA.
DR   RefSeq; XP_002267243.1; XM_002267207.3.
DR   AlphaFoldDB; F6HMV2; -.
DR   STRING; 29760.F6HMV2; -.
DR   PaxDb; 29760-VIT_08s0056g00810-t01; -.
DR   EnsemblPlants; Vitvi08g00070_t001; Vitvi08g00070_P001; Vitvi08g00070.
DR   GeneID; 100251893; -.
DR   Gramene; Vitvi08g00070_t001; Vitvi08g00070_P001; Vitvi08g00070.
DR   KEGG; vvi:100251893; -.
DR   eggNOG; KOG3003; Eukaryota.
DR   HOGENOM; CLU_057217_5_1_1; -.
DR   InParanoid; F6HMV2; -.
DR   OrthoDB; 36313at2759; -.
DR   Proteomes; UP000009183; Chromosome 8.
DR   ExpressionAtlas; F6HMV2; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
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   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU000640};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT   REGION          68..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          142..169
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   338 AA;  37191 MW;  7051359EE3046EE1 CRC64;
     MATLLRAPFT APPPQSLTSI CTQSPKAFHL PLTRRCALNA SRLTSSLRFS PILHIRFLRF
     DPFASNGEAT ETQEVQDSEI EENSDGYIGG AEDATSDSDA PDSDAPNAEE EPASGIIVAL
     RSYKEALVSN DESKAAEIEA FIKFIEDEKI DLEKKVAALS EELSSDKERI LRISADFDNF
     RKRTDRERLS LVTNAQGEVL ENLLPVLDNF ERAKAQIKVE TEGEEKINNS YQSIYKQFVE
     ILGSLGVTPV ETIGNPFDPL FHEAIMREDS TEFEEDVIIQ EFRKGFKLGD RLLRPSMVKV
     SAGPGPAKAE AVGSSEEEAV RVTETETSGE GTPEGESG
//
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