ID   PPI3_SYNY3              Reviewed;         379 AA.
AC   Q55118;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Putative thylakoid lumen peptidyl-prolyl cis-trans isomerase sll0408;
DE            Short=Putative thylakoid lumen PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Putative thylakoid lumen rotamase;
DE   Flags: Precursor;
GN   OrderedLocusNames=sll0408;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   SUBCELLULAR LOCATION IN THYLAKOID.
RX   PubMed=16287171; DOI=10.1002/pmic.200500111;
RA   Srivastava R., Pisareva T., Norling B.;
RT   "Proteomic studies of the thylakoid membrane of Synechocystis sp. PCC
RT   6803.";
RL   Proteomics 5:4905-4916(2005).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Required for the assembly and stabilization of PSII (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid lumen
CC       {ECO:0000305|PubMed:16287171}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA10250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000022; BAA10250.1; ALT_INIT; Genomic_DNA.
DR   PIR; S74332; S74332.
DR   AlphaFoldDB; Q55118; -.
DR   SMR; Q55118; -.
DR   IntAct; Q55118; 3.
DR   STRING; 1148.1001111; -.
DR   PaxDb; Q55118; -.
DR   EnsemblBacteria; BAA10250; BAA10250; BAA10250.
DR   KEGG; syn:sll0408; -.
DR   eggNOG; COG0652; Bacteria.
DR   InParanoid; Q55118; -.
DR   OMA; QFFFFLY; -.
DR   PhylomeDB; Q55118; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0031979; C:plasma membrane-derived thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 1.20.120.290; -; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044665; E_coli_cyclophilin_A-like.
DR   InterPro; IPR023222; PsbQ-like_dom_sf.
DR   PANTHER; PTHR43246; PTHR43246; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   SUPFAM; SSF101112; SSF101112; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; Rotamase; Signal; Thylakoid.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..379
FT                   /note="Putative thylakoid lumen peptidyl-prolyl cis-trans
FT                   isomerase sll0408"
FT                   /id="PRO_0000352737"
FT   DOMAIN          190..378
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   379 AA;  41386 MW;  0C0E52879ECE5B58 CRC64;
     MQIIKTPLGI ITRRGLQLSL LSLLLTMLSL TWAMPGWSLP LNQPMLLGAL AQGNAITDPN
     AILRYALPID NPEVRRLQDS LEDISNHIRA KRWPAIKKDV RAANLTITLK EDKILAGVPA
     DRQPEAETLL GSIKTDLTAL TEAVEAKDKE QVISFRKSAL TAIGDLEALM VTDFPFAIPE
     EFANLPQLKG RATVEMTTNK GPLTIVVDGY SAPINAGNFV DLVQRKFYDG LPFIRSEDFF
     VTQAGDPPGP EAGFIDPQTK EYRAIPLEIL VKGEEGPIYG MTLEDAGMYL PELALPFNAY
     GAIALARPET EPNGGSSQFF FFKFDTELTP PGFNLMDGRY SVFGYVVDGK ETLEQLSEGD
     KIVSAKVISG ADNLVNGNS