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Database: UniProt
Entry: Q5E0C0_ALIF1
LinkDB: Q5E0C0_ALIF1
Original site: Q5E0C0_ALIF1 
ID   Q5E0C0_ALIF1            Unreviewed;       157 AA.
AC   Q5E0C0;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   OrderedLocusNames=VF_A0456 {ECO:0000313|EMBL:AAW87526.1};
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW87526.1, ECO:0000313|Proteomes:UP000000537};
RN   [1] {ECO:0000313|EMBL:AAW87526.1, ECO:0000313|Proteomes:UP000000537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537};
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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|ARBA:ARBA00000971, ECO:0000256|PROSITE-
CC         ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC       {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
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DR   EMBL; CP000021; AAW87526.1; -; Genomic_DNA.
DR   RefSeq; WP_011263320.1; NC_006841.2.
DR   RefSeq; YP_206414.1; NC_006841.2.
DR   AlphaFoldDB; Q5E0C0; -.
DR   STRING; 312309.VF_A0456; -.
DR   EnsemblBacteria; AAW87526; AAW87526; VF_A0456.
DR   KEGG; vfi:VF_A0456; -.
DR   PATRIC; fig|312309.11.peg.3060; -.
DR   eggNOG; COG0545; Bacteria.
DR   HOGENOM; CLU_013615_7_3_6; -.
DR   OMA; FTSMNNQ; -.
DR   OrthoDB; 9814548at2; -.
DR   Proteomes; UP000000537; Chromosome II.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR000774; PPIase_FKBP_N.
DR   PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR   PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF01346; FKBP_N; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000537};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          72..157
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   157 AA;  17096 MW;  CE399CCA94FF19BF CRC64;
     MSKIIITLAI IVLGYMLLQH FVNNPKAAKA NIELGNAFLA ENATKEGVQT TASGLQYLVL
     EEGTGTEHPT AKSKVKVHYH GTTIDGKVFD SSVERGEPIE FGLNQVIKGW TEGVQLMVVG
     QKMRFFIPSD LAYGNRSAGS IQPGSVLIFD VELLDFK
//
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