TC101_PHYPA
ID TC101_PHYPA Reviewed; 919 AA.
AC A9SV59;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Translocase of chloroplast 101, chloroplastic {ECO:0000305};
DE EC=3.6.5.- {ECO:0000305};
DE AltName: Full=101 kDa chloroplast outer envelope protein {ECO:0000305};
GN Name=TOC101 {ECO:0000305};
GN ORFNames=PHYPADRAFT_216050 {ECO:0000312|EMBL:EDQ64902.1};
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; DS545012; EDQ64902.1; -; Genomic_DNA.
DR RefSeq; XP_001770227.1; XM_001770175.1.
DR AlphaFoldDB; A9SV59; -.
DR SMR; A9SV59; -.
DR eggNOG; ENOG502QR60; Eukaryota.
DR HOGENOM; CLU_003856_0_1_1; -.
DR InParanoid; A9SV59; -.
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..919
FT /note="Translocase of chloroplast 101, chloroplastic"
FT /id="PRO_0000451561"
FT TRANSMEM 893..914
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 284..513
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 20..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..300
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 319..323
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 340..343
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 412..415
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 461..463
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 540..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..128
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..565
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 296..301
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 413
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 461..462
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
SQ SEQUENCE 919 AA; 100683 MW; B5437AACC0510B0D CRC64;
MDVENRECSA DLAEELRKLS ASRSLSEEVG VDPALVSEGA PEGVIEGPAV VSSPAKMYTA
LKAVDDEMPP LKSENKAVVE TEKVESKPRG FSAIDFAEED GDSDADAEDE DDEDDEDDDE
DDDDEDDKDM VTAKALAELA NASGKKSSMG AAGPSLPSLP QRPAVRKTAA ATALDTAGRI
TQRPNGAPST QLTATTEENA NSDTAEGNET REKLQNIRVK FLRLAHRLGQ SPQNVVVAQV
LYRLGLAESL RGGNTSNRAG AFSFDRANAL AEEQEAANQE EELDFACTIL VLGKTGVGKS
ATINSIFDDR KSVTSAFKPS TNKVQEIVGT VHGIKVRVID TPGLLPSVAD QQHNERIMGQ
VKKHIKKASP DIVLYFDRLD MQSRDFGDLP LLKTITDLFG AAVWFNAIVV LTHASSAPPD
GPNGVPLSYE MFVAQRSHVV QQTIRQAAGD MRLMNPVSLV ENHPACRTNR NGQRVLPNGQ
IWKPQLLLLC FASKILAEAN SLLKLQETAT PGRPFGQRSR VPPLPFLLSS LLQSRAQLKL
PDEQLDESDE SDDDEEEEDS EADDYDELPP FRPLSKEELE ELTKEQRQDY MDELADRERL
FQKKQYREEM RRRKEMKKRQ AQMSKEELAQ PDEADDEAGQ PAAVPVPMPD MALPPSFDSD
NPTHRYRYLE TANQWLVRPV LETHGWDHDA GYDGFNVEKM FVVKNKIPAS ISGQVTKDKK
ESQVNFEAAA SLKHGEGKVT LTGFDVQTIG KDLAYTLRAE TRFNNFKRNK TTAGVTATYL
NDTIAAGVKL EDRILIGKRV KMVVNGGVLT GKGDKAFGGS LEATLRGKEY PLSRTLSTLG
LSVMDWHGDL AIGGNLQSQF MVGKTMMVGR ANLNNRGSGQ VSIRASSSEQ LQMVLIGIVP
ILRSLINCRF GFGGGQSSQ
