GenomeNet

Database: UniProt
Entry: D6YSE3_WADCW
LinkDB: D6YSE3_WADCW
Original site: D6YSE3_WADCW 
ID   D6YSE3_WADCW            Unreviewed;       256 AA.
AC   D6YSE3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   Name=mip5 {ECO:0000313|EMBL:ADI38988.1};
GN   OrderedLocusNames=wcw_1643 {ECO:0000313|EMBL:ADI38988.1};
OS   Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia.
OX   NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI38988.1, ECO:0000313|Proteomes:UP000001505};
RN   [1] {ECO:0000313|EMBL:ADI38988.1, ECO:0000313|Proteomes:UP000001505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX   PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA   Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA   Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT   "The Waddlia genome: a window into chlamydial biology.";
RL   PLoS ONE 5:E10890-E10890(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001928; ADI38988.1; -; Genomic_DNA.
DR   RefSeq; WP_013182694.1; NZ_LVEB01000003.1.
DR   AlphaFoldDB; D6YSE3; -.
DR   STRING; 716544.wcw_1643; -.
DR   KEGG; wch:wcw_1643; -.
DR   eggNOG; COG0545; Bacteria.
DR   HOGENOM; CLU_013615_0_1_0; -.
DR   OrthoDB; 9814548at2; -.
DR   Proteomes; UP000001505; 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   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 1.10.287.460; Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR000774; PPIase_FKBP_N.
DR   InterPro; IPR036944; PPIase_FKBP_N_sf.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001505};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          148..231
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   256 AA;  28622 MW;  9B639A21D51B37DA CRC64;
     MQTQASKYWR SCCTAATVSL ILFSGCEKKD EEKHSVNEDE IKKISETMGH YVIENLNAQS
     LTLDTESFIK GIEGAKAGQE PPLSKQKFLE LLANYRKKAF EMKSSENLKM AEDYLGDNSN
     SPNIVVLEKG KLHYQRLKPG NGETVSETST PLIQYEGRLI DGQVFDSTGK RGKPAELPLK
     STIPGFRKGI VGMKEGEKRR LFIHPDLGYG ENSRLPPNAL LIFDVEVIKA DAAKKEAKAP
     QKETSMSWLK RWAVPN
//
DBGET integrated database retrieval system