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Database: UniProt
Entry: A0A085A425_9ENTR
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Original site: A0A085A425_9ENTR 
ID   A0A085A425_9ENTR        Unreviewed;       190 AA.
AC   A0A085A425;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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:KFC04970.1};
GN   ORFNames=GTGU_03068 {ECO:0000313|EMBL:KFC04970.1};
OS   Trabulsiella guamensis ATCC 49490.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Trabulsiella.
OX   NCBI_TaxID=1005994 {ECO:0000313|EMBL:KFC04970.1, ECO:0000313|Proteomes:UP000028630};
RN   [1] {ECO:0000313|EMBL:KFC04970.1, ECO:0000313|Proteomes:UP000028630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49490 {ECO:0000313|EMBL:KFC04970.1,
RC   ECO:0000313|Proteomes:UP000028630};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFC04970.1}.
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DR   EMBL; JMTB01000093; KFC04970.1; -; Genomic_DNA.
DR   RefSeq; WP_038158660.1; NZ_JMTB01000093.1.
DR   AlphaFoldDB; A0A085A425; -.
DR   eggNOG; COG0652; Bacteria.
DR   OrthoDB; 9807797at2; -.
DR   Proteomes; UP000028630; Unassembled WGS sequence.
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:KFC04970.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
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_5006512877"
FT   DOMAIN          35..188
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   190 AA;  20410 MW;  DE4BBAAD59EEF895 CRC64;
     MLKSTLAAVA AVFAFSAISP AALAAKGDPH VLLTTSAGNI ELELDKQKAP VSVENFLNYV
     NSGFYNNTTF HRVIPGFMVQ GGGFNEQMQQ KQPNPPIKNE ADNGLRNTRG TISMARTADK
     DSATSQFFIN VADNAFLDHG QRDFGYAVFG KVVKGMDVAD KISQVPTHDV GPYQNVPSKP
     VVILSAKVLP
//
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