TIC55_PEA
ID TIC55_PEA Reviewed; 553 AA.
AC O49931;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein TIC 55, chloroplastic;
DE AltName: Full=Rieske iron-sulfur protein TIC55;
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 55;
DE Short=PsTIC55;
DE Flags: Precursor;
GN Name=TIC55;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-80, INTERACTION WITH
RP TIC110, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=9405363; DOI=10.1093/emboj/16.24.7342;
RA Caliebe A., Grimm R., Kaiser G., Luebeck J., Soll J., Heins L.;
RT "The chloroplastic protein import machinery contains a Rieske-type iron-
RT sulfur cluster and a mononuclear iron-binding protein.";
RL EMBO J. 16:7342-7350(1997).
RN [2]
RP INTERACTION WITH TIC62.
RX PubMed=12426385; DOI=10.1093/emboj/cdf621;
RA Kuechler M., Decker S., Hoermann F., Soll J., Heins L.;
RT "Protein import into chloroplasts involves redox-regulated proteins.";
RL EMBO J. 21:6136-6145(2002).
RN [3]
RP REVIEW.
RX PubMed=20100520; DOI=10.1016/j.bbamcr.2010.01.015;
RA Kovacs-Bogdan E., Soll J., Bolter B.;
RT "Protein import into chloroplasts: the Tic complex and its regulation.";
RL Biochim. Biophys. Acta 1803:740-747(2010).
CC -!- FUNCTION: Involved in protein precursor import into chloroplasts. Part
CC of the redox regulon consisting of TIC32, TIC 55 and TIC62.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- SUBUNIT: Part of the Tic complex. Interacts with TIC62 and TIC110.
CC {ECO:0000269|PubMed:12426385, ECO:0000269|PubMed:9405363}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:9405363}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9405363}.
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DR EMBL; AJ000520; CAA04157.1; -; mRNA.
DR PIR; T06499; T06499.
DR AlphaFoldDB; O49931; -.
DR SMR; O49931; -.
DR IntAct; O49931; 2.
DR TCDB; 3.A.9.1.1; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010277; F:chlorophyllide a oxygenase [overall] activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR013626; PaO.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF08417; PaO; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Chloroplast; Direct protein sequencing; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Plastid; Plastid inner membrane;
KW Protein transport; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..553
FT /note="Protein TIC 55, chloroplastic"
FT /id="PRO_0000413680"
FT TOPO_DOM 61..492
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..518
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..553
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT DOMAIN 103..208
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 144
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 146
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 163
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 166
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 257
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
SQ SEQUENCE 553 AA; 62069 MW; 680D595446824D39 CRC64;
MALALASANS FLLPTKTHFA LHVSPPPSKK TLLCTNPSSN FSFNKALSSR RRKQAWCVAA
AADVKDATLL DGEEDQKVLV GPSSEQERKG EREVADYDWT EEWYPLYLTK NVPHDAPLGL
KVYDKNIVLF RDGNDQFQCY EDRCPHRLAK LSEGQLIDGR LECLYHGWQF EGEGKCVKIP
QLPADAKIPK SACVKTYEVR DSQGVLWVWM SRKTPPNVSK IPWFENFARP GFQDISTTHE
LPYDHSILLE NLMDPAHVPI SHDRTDWSAK REDAQALGFE VTERTDRGFA GWWGREKDGS
KPNFLRFEAP CVLQNNREIV DKNGEINHFS GLFLCRPTGQ GKSMLIVRFG ATKRSPLIKL
FPEWYFHQNA SKVFEQDMGF LSSQNEILLK EKVPTKELYL NLKSSDTWVA EYRKWMDKVG
HGMPYHFGHS TISLPEEPAV VEHAPAGLVA GLSASSPAKG GIGTMHAPNL ANRYFRHVIH
CKGCSSAIKA FQIWKNVLSG VVVALAALAI LVSGRQWKVL LLASASLCSV GVYACSTAIA
MNTTNFIRVH RRL
