ID U3U417_9ENTR Unreviewed; 190 AA.
AC U3U417;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN Name=ppiA {ECO:0000313|EMBL:BAN98878.1};
GN ORFNames=E05_41120 {ECO:0000313|EMBL:BAN98878.1};
OS Plautia stali symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN98878.1, ECO:0000313|Proteomes:UP000016901};
RN [1] {ECO:0000313|EMBL:BAN98878.1, ECO:0000313|Proteomes:UP000016901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT lipopolysaccharide.";
RL Microbiol. Res. 167:48-54(2011).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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 Evidence={ECO:0000256|RuleBase:RU363019};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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DR EMBL; AP012551; BAN98878.1; -; Genomic_DNA.
DR AlphaFoldDB; U3U417; -.
DR KEGG; psts:E05_41120; -.
DR eggNOG; COG0652; Bacteria.
DR HOGENOM; CLU_012062_16_9_6; -.
DR Proteomes; UP000016901; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01920; cyclophilin_EcCYP_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044665; E_coli_cyclophilin_A-like.
DR PANTHER; PTHR43246:SF12; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A; 1.
DR PANTHER; PTHR43246; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE CYP38, CHLOROPLASTIC; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:BAN98878.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000016901};
KW Rotamase {ECO:0000256|RuleBase:RU363019};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU363019}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT CHAIN 25..190
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT /id="PRO_5006530786"
FT DOMAIN 35..188
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 190 AA; 20401 MW; C358CDC7643D196B CRC64;
MLKRTLTAAV ALLALSSVSA SALAAKGDTH VLLTTSAGNI ELELDNQKAP VSVKNFVDYV
NNGFYNNTIF HRVIPGFMIQ GGGFTADMQQ KQTNAPIKNE ADNGLRNLRG TISMARTAEK
DSATSQFFLN VADNAFLDHG QRDFGYAVFG KVVKGMDVID KIAQVPTKDV GPYQNVPSKP
VVITSAKVLP
//
