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Database: UniProt
Entry: A0A088QIT5_9CORY
LinkDB: A0A088QIT5_9CORY
Original site: A0A088QIT5_9CORY 
ID   A0A088QIT5_9CORY        Unreviewed;       119 AA.
AC   A0A088QIT5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   ORFNames=DR71_646 {ECO:0000313|EMBL:AIN83215.1};
OS   Corynebacterium sp. ATCC 6931.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1487956 {ECO:0000313|EMBL:AIN83215.1, ECO:0000313|Proteomes:UP000029247};
RN   [1] {ECO:0000313|EMBL:AIN83215.1, ECO:0000313|Proteomes:UP000029247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6931 {ECO:0000313|Proteomes:UP000029247};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA   Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (JUL-2014) 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, 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; CP008913; AIN83215.1; -; Genomic_DNA.
DR   RefSeq; WP_005511805.1; NZ_CP008913.1.
DR   AlphaFoldDB; A0A088QIT5; -.
DR   STRING; 1487956.DR71_646; -.
DR   GeneID; 64051861; -.
DR   KEGG; coa:DR71_646; -.
DR   eggNOG; COG0545; Bacteria.
DR   HOGENOM; CLU_013615_12_0_11; -.
DR   Proteomes; UP000029247; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
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   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:UP000029247};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          33..119
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   119 AA;  12683 MW;  EBFFFCF038653BF2 CRC64;
     MSKPELTAKS GPAPTELVIN DLTVGDGKEA TPGARVEVHY VGVDYETGEE FDSSWNRGQS
     IEFPLNGLIA GWQEGIPGMK VGGRRELICP PEKAYGPAGA GHFLSGKTLV FVIDLLDVK
//
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