TC125_PHYPA
ID TC125_PHYPA Reviewed; 1141 AA.
AC A9SY64; Q6RJN8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Translocase of chloroplast 125, chloroplastic {ECO:0000305};
DE Short=PpTOC125 {ECO:0000303|PubMed:15010601};
DE EC=3.6.5.- {ECO:0000305};
DE AltName: Full=125 kDa chloroplast outer envelope protein {ECO:0000305};
GN Name=TOC125 {ECO:0000303|PubMed:15010601};
GN ORFNames=PHYPA_009855 {ECO:0000312|EMBL:PNR50669.1},
GN PHYPADRAFT_216964 {ECO:0000312|EMBL:EDQ63890.1};
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 [MRNA], AND FUNCTION.
RX PubMed=15010601; DOI=10.1023/b:plan.0000019065.31490.06;
RA Hofmann N.R., Theg S.M.;
RT "Physcomitrella patens as a model for the study of chloroplast protein
RT transport: conserved machineries between vascular and non-vascular
RT plants.";
RL Plant Mol. Biol. 53:621-632(2003).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=cv. Gransden 2004;
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
CC -!- FUNCTION: GTPase involved in protein precursor import into chloroplasts
CC (Probable). Seems to recognize chloroplast-destined precursor proteins
CC and regulate their presentation to the translocation channel through
CC GTP hydrolysis (Probable). Probably specialized in the import of
CC nuclear encoded non-photosynthetic preproteins from the cytoplasm to
CC the chloroplast (Probable). {ECO:0000305|PubMed:15010601}.
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:0000305}.
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; AY496562; AAS47583.1; -; mRNA.
DR EMBL; DS545025; EDQ63890.1; -; Genomic_DNA.
DR EMBL; ABEU02000007; PNR50669.1; -; Genomic_DNA.
DR RefSeq; XP_001771330.1; XM_001771278.1.
DR AlphaFoldDB; A9SY64; -.
DR SMR; A9SY64; -.
DR STRING; 3218.PP1S136_59V6.1; -.
DR EnsemblPlants; Pp3c7_3450V3.1; Pp3c7_3450V3.1; Pp3c7_3450.
DR EnsemblPlants; Pp3c7_3450V3.2; Pp3c7_3450V3.2; Pp3c7_3450.
DR Gramene; Pp3c7_3450V3.1; Pp3c7_3450V3.1; Pp3c7_3450.
DR Gramene; Pp3c7_3450V3.2; Pp3c7_3450V3.2; Pp3c7_3450.
DR eggNOG; ENOG502QR60; Eukaryota.
DR HOGENOM; CLU_003856_0_0_1; -.
DR InParanoid; A9SY64; -.
DR OrthoDB; 944325at2759; -.
DR Proteomes; UP000006727; Chromosome 7.
DR GO; GO:0009707; C:chloroplast outer membrane; IBA:GO_Central.
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:0045037; P:protein import into chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0045036; P:protein targeting to chloroplast; IBA:GO_Central.
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 2: Evidence at transcript level;
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..1141
FT /note="Translocase of chloroplast 125, chloroplastic"
FT /id="PRO_0000451563"
FT TRANSMEM 1116..1136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 505..734
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..521
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 541..545
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 561..564
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 633..636
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 682..684
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 758..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..355
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..788
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 517..522
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 634
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 682..683
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT CONFLICT 849
FT /note="E -> G (in Ref. 1; AAS47583)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1141 AA; 125252 MW; 53B03B7DB2EC978D CRC64;
MDALRKLGSL GRRRDEVDTA SSPLKNEASA AEIPRDPVQI SGKDEASPSG LTPIRVRVPE
DVRSESEVKR DGDEESVGSG ESFDSALERM EASSITSFEP PSPMESIDGR FQFEDGVRED
LAESGLDGNF SYDDDDDDEE EEEDGSEEGE STSSSIINSE YSSSASNTED EMDISGYGAS
SARTMLVSND ASKSDEEAID EPKYKLRNVV TGEENMSGGL SVENEARGVA LSSWKSELED
FYEASLEDND VQEELAEKII KVASEQNDEE DEEVHFPVIA NELPGRITRN RTMIDSPAHL
YSAVKAVDST LPALKSESTK SITQGFVEAE EAESDVFTEG EDGYDDEDED GDIQMDVSQA
TEKSGTPDES ESNPSMGAGG PRLPSLPQRS SARRSAATTA TGVPRPNTAS STQSAATSDA
SISSESSEAN EIREKLQNIR IKFLRLARRL NQSPQNVVVA QVLYRLGLAE SLRGGSSLNR
TRAFSFDHAN ALAEEQEAAK YEDLDFACTI LVLGKTGVGK SATINSIFDE CKTVTSAYYP
STTKVHEVSG TVLGVKVRFI DTPGLLPSTA DQRHNKNIMR QVKKYIKKVS PDIVLYFDRM
DMQTRDSGDV PLLRTITDVF GAAVWFNATV VLTHASKAPP DGSNGTPMSY DYFVAQRSHF
VQQTIRQAAG DARLQNPVSL VENHPACRIN RSGQRVLPNG QPWKQQLLLL CFASKILAEA
NTLLKLQEAS TPGKPFGQRS RVPPLPYLLS SLLQSRAQLK MPDEQHGESE DSDDDSDEED
EEEGDEYDDL PPFRPLSKQE LEDLSKEQRQ EYAEELADRE RLFQKKQYRE QIRRRRERKK
QASVMSKEEP SIPGDGAEDE SGQPATVAVP MPDMALPPSF DSDNPTHRYR YLETANQWLV
RPVLETHGWD HDAGYDGFNV EKMFVVKEKI PASVSGQVTK DKKEAQVNFE AAASLRHGEG
KVTLTGFDVQ TIGKDLAYTV RAETRFNNFK RNKTTAGVTA TYLNDTIAAG VKLEDRVLIG
KRVKLVVNGG VLTGKGDKAY GGSLEATLRG KEYPLSRTLS TLGLSVMDWH GDLAIGGNLQ
SQFMVGKTMM VGRANLNNRG SGQVSIRASS SEQLQMVLIG IVPILRSLIN CRFGFGGQPQ
Q
