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Database: UniProt
Entry: F8AD53_THEID
LinkDB: F8AD53_THEID
Original site: F8AD53_THEID 
ID   F8AD53_THEID            Unreviewed;       154 AA.
AC   F8AD53;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   OrderedLocusNames=Thein_0909 {ECO:0000313|EMBL:AEH44785.1};
OS   Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812).
OC   Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC   Thermodesulfobacteriales; Thermodesulfatatoraceae; Thermodesulfatator.
OX   NCBI_TaxID=667014 {ECO:0000313|EMBL:AEH44785.1, ECO:0000313|Proteomes:UP000006793};
RN   [1] {ECO:0000313|Proteomes:UP000006793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC   {ECO:0000313|Proteomes:UP000006793};
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders L.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermodesulfatator indicus DSM 15286.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEH44785.1, ECO:0000313|Proteomes:UP000006793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC   {ECO:0000313|Proteomes:UP000006793};
RX   PubMed=22768359; DOI=10.4056/sigs.2665915;
RA   Anderson I., Saunders E., Lapidus A., Nolan M., Lucas S., Tice H.,
RA   Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA   Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Chang Y.J.,
RA   Brambilla E.M., Rohde M., Spring S., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of the thermophilic sulfate-reducing ocean
RT   bacterium Thermodesulfatator indicus type strain (CIR29812(T)).";
RL   Stand. Genomic Sci. 6:155-164(2012).
CC   -!- FUNCTION: Also involved in hydrogenase metallocenter assembly, probably
CC       by participating in the nickel insertion step. This function in
CC       hydrogenase biosynthesis requires chaperone activity and the presence
CC       of the metal-binding domain, but not PPIase activity.
CC       {ECO:0000256|ARBA:ARBA00037071}.
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; CP002683; AEH44785.1; -; Genomic_DNA.
DR   RefSeq; WP_013907528.1; NC_015681.1.
DR   AlphaFoldDB; F8AD53; -.
DR   STRING; 667014.Thein_0909; -.
DR   PaxDb; 667014-Thein_0909; -.
DR   KEGG; tid:Thein_0909; -.
DR   PATRIC; fig|667014.3.peg.932; -.
DR   eggNOG; COG1047; Bacteria.
DR   HOGENOM; CLU_098197_2_1_0; -.
DR   InParanoid; F8AD53; -.
DR   OrthoDB; 9808891at2; -.
DR   Proteomes; UP000006793; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProt.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR47861; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1.
DR   PANTHER; PTHR47861:SF3; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1.
DR   Pfam; PF00254; FKBP_C; 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:UP000006793};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          7..84
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   154 AA;  16607 MW;  641EED68E4063939 CRC64;
     MRKVKLGDVV SIHCVGKLAN GEVFESTEGG PPFQFQVGSP EIIPGLSEAV IGMAEGEEKE
     ITLSPDKAFG ERDERLVKVV PKDALSLDTE PQVGMMLNLV FNTEQGEVTV PATITNIDEE
     NLTLDLNPPL AGETVTFYIK VVEIENGESP IITP
//
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