ID H5XRP9_9FIRM Unreviewed; 327 AA.
AC H5XRP9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=DesyoDRAFT_0076 {ECO:0000313|EMBL:EHQ87308.1};
OS Desulfosporosinus youngiae DSM 17734.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768710 {ECO:0000313|EMBL:EHQ87308.1, ECO:0000313|Proteomes:UP000005104};
RN [1] {ECO:0000313|EMBL:EHQ87308.1, ECO:0000313|Proteomes:UP000005104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17734 {ECO:0000313|EMBL:EHQ87308.1,
RC ECO:0000313|Proteomes:UP000005104};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Land M.L., Hauser L., Pester M.,
RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA Woyke T.J.;
RT "The Noncontiguous Finished genome of Desulfosporosinus youngiae DSM
RT 17734.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CM001441; EHQ87308.1; -; Genomic_DNA.
DR AlphaFoldDB; H5XRP9; -.
DR STRING; 768710.DesyoDRAFT_0076; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_5_2_9; -.
DR Proteomes; UP000005104; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF13616; Rotamase_3; 1.
DR Pfam; PF13624; SurA_N_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00278}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005104};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..275
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 327 AA; 36443 MW; 9E04EF5FD405A80B CRC64;
MIYYSHVKLK GCVNMKKPRV GFVFGVLALM IMTTGCSSLV GGKWAVKVNE TPILVKDYDV
RVSEAQKVYE KQGMKFDTDQ GKEALPQIKS MLLERMIEGE LIAQEVKNLS LNSEDAKVKE
QEEIIKKNMG NEATFQDTLK QQGMTEPELR NFLMVYEKVT GDVNVNETEV KAFFDKNISY
YSQPESVKAR HILVKTEDEA KAIIAQLSAG ADFEQLAKEK SIEPGAKESG GDLGTFTKGR
MVPEFEAAAF AQKVGTFSTA PVKTEFGYHV IKVEEHTVAA APEYAKVQGQ VGQDALNQAK
DAKFQTYFDE LRKNAKIEYS QGYKPAS
//
