TC108_PHYPA
ID TC108_PHYPA Reviewed; 994 AA.
AC A9SY65;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Translocase of chloroplast 108, chloroplastic {ECO:0000305};
DE EC=3.6.5.- {ECO:0000305};
DE AltName: Full=108 kDa chloroplast outer envelope protein {ECO:0000305};
GN Name=TOC108 {ECO:0000305};
GN ORFNames=PHYPADRAFT_189669 {ECO:0000312|EMBL:EDQ63891.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
CC -!- FUNCTION: GTPase involved in protein precursor import into
CC chloroplasts. Seems to recognize chloroplast-destined precursor
CC proteins and regulate their presentation to the translocation channel
CC through GTP hydrolysis. Probably specialized in the import of nuclear
CC encoded non-photosynthetic preproteins from the cytoplasm to the
CC chloroplast. {ECO:0000250|UniProtKB:A9SY64}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O23680};
CC Note=Binds 1 Mg(2+) ion by subunit. {ECO:0000250|UniProtKB:O23680};
CC -!- SUBUNIT: Part of the TOC core complex. {ECO:0000250|UniProtKB:A9SY64}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC TOC159 subfamily. {ECO:0000305}.
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DR EMBL; DS545025; EDQ63891.1; -; Genomic_DNA.
DR RefSeq; XP_001771331.1; XM_001771279.1.
DR AlphaFoldDB; A9SY65; -.
DR SMR; A9SY65; -.
DR eggNOG; ENOG502QR60; Eukaryota.
DR HOGENOM; CLU_003856_0_1_1; -.
DR InParanoid; A9SY65; -.
DR Proteomes; UP000006727; Unplaced.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045036; P:protein targeting to chloroplast; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006703; G_AIG1.
DR InterPro; IPR045058; GIMA/IAN/Toc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR024283; TOC159_MAD.
DR InterPro; IPR005690; Toc86_159.
DR PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR Pfam; PF11886; TOC159_MAD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00993; 3a0901s04IAP86; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 3: Inferred from homology;
KW Chloroplast; GTP-binding; Hydrolase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Plastid; Plastid outer membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..994
FT /note="Translocase of chloroplast 108, chloroplastic"
FT /id="PRO_0000451562"
FT TRANSMEM 969..989
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 360..589
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 14..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..376
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 395..399
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 416..419
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 488..491
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 537..539
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 616..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..641
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 372..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 489
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 537..538
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
SQ SEQUENCE 994 AA; 108396 MW; 333F477BE6DEC899 CRC64;
MAELEKLAAA RLEKEASNNT VNPVREVSED DVKDVSGETT VVTTSISEGA NESLSKKEDE
PALIGSNVPE ELEGNSLEVQ SAITTDLEKV SSTPTPSNAE KESPEATEVR IVEEGKLEKA
DPSVVNEELS KEILEDPEVV PSPAKMYTAL KAVDGDMPVL KSENGNDGDT DANTADEDNE
NDEDDVDEDE DEDDADMDTA KALAELAMTA GKSGNPAFSG TKPSMGAAGP SLPSLPQRPA
VRKPIAATAS DSPGRNTQRP NGALSTQITS TTDESASSDA AEGDETREKL QNIRVKFLRL
AHRLGQSPQN VVVAQVLYRL GLAESLRGGS APNRSGAFSF DRANALAEEQ EAANQEEELD
FACTILVLGK TGVGKSSTIN SIFDERKSVT SAFKPSTNKV QEVIGTVHGI KVRVIDTPGL
LPSVADQQHN ERIMGQVKKY IKKASPDIVL YFDRLDMQSR DFGDLPLLRT ITDLFGAAVW
FNAIVVLTHA SSAPPDGPNG VPLSYEMFVA QRSHVVQQTI RQAAGDMRLM NPVSLVENHP
ACRTNRTGQR VLPNGQIWKP QLLLLCFASK ILAEANSLLK LQETTAPGRP FGQRSRVPPL
PFLLSSLLQS RAQLKLPDEQ AGESDESDDD EEEEDSDADD YDELPPFRPL SKEELEDLTK
EQREDYMEEL ADRERMFQKK QYREEIRRRK EAKKRQAQMS KEELAEAEEA EDEAGNAAAV
PVPMPDMALP PSFDSDNPTH RYRYLETANQ WLVRPVLETH GWDHDAGYDG FNVEKMFVVK
EKIPASVSGQ VTKDKKEAQV NFEAAASLRH GEGKVTLTGF DVQTIGKDLA YTVRAETRFN
NFKRNKTTAG VTATYLNDTI AAGVKLEDRV LIGKRVKLVV NGGVLTGKGD KAYGGSLEAT
LRGKEYPLSR TLSTLGLSVM DWHGDLAIGG NLQSQFMVGK TMMVGRANLN NRGSGQVSIR
ASSSEQLQMV LIGIVPILRS LINCRFGFGG QSQQ
