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
//