| General information | | DisProt: | DP00609 | | Name: | Translocase of chloroplast 159, chloroplastic | | Synonym(s): | Translocon at the outer envelope membrane of chloroplasts 159
AtToc159
TC159_ARATH
Translocase of chloroplast 160, chloroplastic;AtToc160
Translocase of chloroplast 86, chloroplastic; AtToc86
159 kDa chloroplast outer envelope protein
Plastid protein import 2
| | First appeared in release: | Release 5.1 (05/28/2010) | | UniProt: | O81283 | | UniGene: | At.24962 | | SwissProt: | TC159_ARATH | | TrEMBL: | | | NCBI (GI): | 75100143 | | Source organism: | Arabidopsis thaliana (Mouse-ear cress) | | Sequence length: | 1503 | | Percent disordered: | 56% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MDSKSVTPEP TNPFYASSGQ SGKTYASVVA AAAAAAADKE DGGAVSSAKE LDSSSEAVSG - 60
NSDKVGADDL SDSEKEKPNL VGDGKVSDEV DGSLKEDSTT PEATPKPEVV SGETIGVDDV - 120
SSLSPKPEAV SDGVGVVEEN KKVKEDVEDI KDDGESKIEN GSVDVDVKQA STDGESESKV - 180
KDVEEEDVGT KKDDEGESEL GGKVDVDDKS DNVIEEEGVE LTDKGDVIVN SSPVESVHVD - 240
VAKPGVVVVG DAEGSEELKI NADAETLEVA NKFDQIGDDD SGEFEPVSDK AIEEVEEKFT - 300
SESDSIADSS KLESVDTSAV EPEVVAAESG SEPKDVEKAN GLEKGMTYAE VIKAASAVAD - 360
NGTKEEESVL GGIVDDAEEG VKLNNKGDFV VDSSAIEAVN VDVAKPGVVV VGDVEVSEVL - 420
ETDGNIPDVH NKFDPIGQGE GGEVELESDK ATEEGGGKLV SEGDSMVDSS VVDSVDADIN - 480
VAEPGVVVVG AAKEAVIKED DKDDEVDKTI SNIEEPDDLT AAYDGNFELA VKEISEAAKV - 540
EPDEPKVGVE VEELPVSESL KVGSVDAEED SIPAAESQFE VRKVVEGDSA EEDENKLPVE - 600
DIVSSREFSF GGKEVDQEPS GEGVTRVDGS ESEEETEEMI FGSSEAAKQF LAELEKASSG - 660
IEAHSDEANI SNNMSDRIDG QIVTDSDEDV DTEDEGEEKM FDTAALAALL KAATGGGSSE - 720
GGNFTITSQD GTKLFSMDRP AGLSSSLRPL KPAAAPRANR SNIFSNSNVT MADETEINLS - 780
EEEKQKLEKL QSLRVKFLRL LQRLGHSAED SIAAQVLYRL ALLAGRQAGQ LFSLDAAKKK - 840
AVESEAEGNE ELIFSLNILV LGKAGVGKSA TINSILGNQI ASIDAFGLST TSVREISGTV - 900
NGVKITFIDT PGLKSAAMDQ STNAKMLSSV KKVMKKCPPD IVLYVDRLDT QTRDLNNLPL - 960
LRTITASLGT SIWKNAIVTL THAASAPPDG PSGTPLSYDV FVAQCSHIVQ QSIGQAVGDL - 1020
RLMNPSLMNP VSLVENHPLC RKNREGVKVL PNGQTWRSQL LLLCYSLKVL SETNSLLRPQ - 1080
EPLDHRKVFG FRVRSPPLPY LLSWLLQSRA HPKLPGDQGG DSVDSDIEID DVSDSEQEDG - 1140
EDDEYDQLPP FKPLRKTQLA KLSNEQRKAY FEEYDYRVKL LQKKQWREEL KRMKEMKKNG - 1200
KKLGESEFGY PGEEDDPENG APAAVPVPLP DMVLPPSFDS DNSAYRYRYL EPTSQLLTRP - 1260
VLDTHGWDHD CGYDGVNAEH SLALASRFPA TATVQVTKDK KEFNIHLDSS VSAKHGENGS - 1320
TMAGFDIQNV GKQLAYVVRG ETKFKNLRKN KTTVGGSVTF LGENIATGVK LEDQIALGKR - 1380
LVLVGSTGTM RSQGDSAYGA NLEVRLREAD FPIGQDQSSF GLSLVKWRGD LALGANLQSQ - 1440
VSVGRNSKIA LRAGLNNKMS GQITVRTSSS DQLQIALTAI LPIAMSIYKS IRPEATNDKY - 1500
SMY
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| Functional narrative |
GTPase involved in protein precursor import into chloroplasts. Seems to recognize chloroplast-destined precursor proteins and regulate their presentation to the translocation channel through GTP hydrolysis. Required for chloroplast biogenesis. Probably specialized in the import of nuclear encoded photosynthetic preproteins from the cytoplasm to the chloroplast.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | N-terminal acidic (A-) domain | | Location: | 1 - 727 | | Length: | 727 | | Region sequence: |
MDSKSVTPEPTNPFYASSGQSGKTYASVVAAAAAAAADKEDGGAVSSAKELDSSSEAVSG
NSDKVGADDLSDSEKEKPNLVGDGKVSDEVDGSLKEDSTTPEATPKPEVVSGETIGVDDV
SSLSPKPEAVSDGVGVVEENKKVKEDVEDIKDDGESKIENGSVDVDVKQASTDGESESKV
KDVEEEDVGTKKDDEGESELGGKVDVDDKSDNVIEEEGVELTDKGDVIVNSSPVESVHVD
VAKPGVVVVGDAEGSEELKINADAETLEVANKFDQIGDDDSGEFEPVSDKAIEEVEEKFT
SESDSIADSSKLESVDTSAVEPEVVAAESGSEPKDVEKANGLEKGMTYAEVIKAASAVAD
NGTKEEESVLGGIVDDAEEGVKLNNKGDFVVDSSAIEAVNVDVAKPGVVVVGDVEVSEVL
ETDGNIPDVHNKFDPIGQGEGGEVELESDKATEEGGGKLVSEGDSMVDSSVVDSVDADIN
VAEPGVVVVGAAKEAVIKEDDKDDEVDKTISNIEEPDDLTAAYDGNFELAVKEISEAAKV
EPDEPKVGVEVEELPVSESLKVGSVDAEEDSIPAAESQFEVRKVVEGDSAEEDENKLPVE
DIVSSREFSFGGKEVDQEPSGEGVTRVDGSESEEETEEMIFGSSEAAKQFLAELEKASSG
IEAHSDEANISNNMSDRIDGQIVTDSDEDVDTEDEGEEKMFDTAALAALLKAATGGGSSE
GGNFTIT | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Substrate/ligand binding
Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 8; )
| References:
- Richardson LG, Jelokhani-Niaraki M, Smith MD. "The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains." BMC Biochem. 2009; 10(1): 35. PubMed: 20042108
| Comments:The A-domain was shown experimentally to be disordered under non-denaturing conditions, and underwent structural changes characteristic of IDPs at extremes of temperature and pH. Furthermore, in the presence of 50% TFE, the A-domain gained considerable structure.
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| Region 2 | | Type: | Disordered | | Name: | A1 | | Location: | 163 - 374 | | Length: | 212 | | Region sequence: |
VDVDVKQASTDGESESKVKDVEEEDVGTKKDDEGESELGGKVDVDDKSDNVIEEEGVELT
DKGDVIVNSSPVESVHVDVAKPGVVVVGDAEGSEELKINADAETLEVANKFDQIGDDDSG
EFEPVSDKAIEEVEEKFTSESDSIADSSKLESVDTSAVEPEVVAAESGSEPKDVEKANGL
EKGMTYAEVIKAASAVADNGTKEEESVLGGIV | | Modification type: | Isoform
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 3; )
| References:
- Richardson LG, Jelokhani-Niaraki M, Smith MD. "The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains." BMC Biochem. 2009; 10(1): 35. PubMed: 20042108
| Comments:
|
| Region 3 | | Type: | Disordered | | Name: | A2 | | Location: | 408 - 627 | | Length: | 220 | | Region sequence: |
VVVVGDVEVSEVLETDGNIPDVHNKFDPIGQGEGGEVELESDKATEEGGGKLVSEGDSMV
DSSVVDSVDADINVAEPGVVVVGAAKEAVIKEDDKDDEVDKTISNIEEPDDLTAAYDGNF
ELAVKEISEAAKVEPDEPKVGVEVEELPVSESLKVGSVDAEEDSIPAAESQFEVRKVVEG
DSAEEDENKLPVEDIVSSREFSFGGKEVDQEPSGEGVTRV | | Modification type: | Isoform
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
| References:
- Richardson LG, Jelokhani-Niaraki M, Smith MD. "The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains." BMC Biochem. 2009; 10(1): 35. PubMed: 20042108
| Comments:
|
| Region 4 | | Type: | Disordered | | Name: | A3 | | Location: | 639 - 839 | | Length: | 201 | | Region sequence: |
MIFGSSEAAKQFLAELEKASSGIEAHSDEANISNNMSDRIDGQIVTDSDEDVDTEDEGEE
KMFDTAALAALLKAATGGGSSEGGNFTITSQDGTKLFSMDRPAGLSSSLRPLKPAAAPRA
NRSNIFSNSNVTMADETEINLSEEEKQKLEKLQSLRVKFLRLLQRLGHSAEDSIAAQVLY
RLALLAGRQAGQLFSLDAAKK | | Modification type: | Isoform
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
| References:
- Richardson LG, Jelokhani-Niaraki M, Smith MD. "The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains." BMC Biochem. 2009; 10(1): 35. PubMed: 20042108
| Comments:
|
| References |
- Richardson LG, Jelokhani-Niaraki M, Smith MD. "The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains." BMC Biochem. 2009; 10(1): 35. PubMed: 20042108
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| Comments |
Additional UniGene ID: Rra.6577 and Rsa.11612
[PMID 20042108 ]
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