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Database: UniProt
Entry: Q8A607_BACTN
LinkDB: Q8A607_BACTN
Original site: Q8A607_BACTN 
ID   Q8A607_BACTN            Unreviewed;       191 AA.
AC   Q8A607;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   OrderedLocusNames=BT_2079 {ECO:0000313|EMBL:AAO77186.1};
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO77186.1, ECO:0000313|Proteomes:UP000001414};
RN   [1] {ECO:0000313|EMBL:AAO77186.1, ECO:0000313|Proteomes:UP000001414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
RN   [2] {ECO:0000313|EMBL:AAO77186.1, ECO:0000313|Proteomes:UP000001414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; AE015928; AAO77186.1; -; Genomic_DNA.
DR   RefSeq; NP_810992.1; NC_004663.1.
DR   RefSeq; WP_008761032.1; NZ_UYXG01000005.1.
DR   AlphaFoldDB; Q8A607; -.
DR   STRING; 226186.BT_2079; -.
DR   PaxDb; 226186-BT_2079; -.
DR   EnsemblBacteria; AAO77186; AAO77186; BT_2079.
DR   GeneID; 60928068; -.
DR   KEGG; bth:BT_2079; -.
DR   PATRIC; fig|226186.12.peg.2140; -.
DR   eggNOG; COG1047; Bacteria.
DR   HOGENOM; CLU_098197_0_0_10; -.
DR   InParanoid; Q8A607; -.
DR   OMA; HSHEGGC; -.
DR   OrthoDB; 9808891at2; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.10.330; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR048261; SlpA/SlyD-like_ins_sf.
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:UP000001414};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          6..85
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   191 AA;  20834 MW;  EAED2A5F7EB8C8B0 CRC64;
     METVENKYIT VAYKLYTVED GEKELFEETN AEHPFQFISG LGTTLESFEN QITALSKGDK
     FDFTIPADEA YGAYDEQHVF DLPKNIFEID GKFDSERVTE GSIVPLMTGD GQRVNASVVE
     IKPDVVVVDL NHPLAGADLI FEGEVIESRP ATNEEIQELV KMMSGEGCGC GCDSCGSDCG
     DDCGCEGGHC H
//
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