FKBP_CORGL
ID FKBP_CORGL Reviewed; 118 AA.
AC P42458;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable FK506-binding protein;
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
GN OrderedLocusNames=Cgl0830, cg0950;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=7522844; DOI=10.1099/13500872-140-8-1817;
RA Eikmanns B.J., Thum-Schmitz N., Eggeling L., Luedtke K.U., Sahm H.;
RT "Nucleotide sequence, expression and transcriptional analysis of the
RT Corynebacterium glutamicum gltA gene encoding citrate synthase.";
RL Microbiology 140:1817-1828(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: PPIases accelerate the folding of proteins.
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 -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; X66112; CAA46903.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98223.1; -; Genomic_DNA.
DR EMBL; BX927150; CAF19536.1; -; Genomic_DNA.
DR PIR; I40718; I40718.
DR RefSeq; NP_600059.1; NC_003450.3.
DR RefSeq; WP_003858324.1; NC_006958.1.
DR AlphaFoldDB; P42458; -.
DR SMR; P42458; -.
DR STRING; 196627.cg0950; -.
DR GeneID; 58311150; -.
DR KEGG; cgb:cg0950; -.
DR KEGG; cgl:Cgl0830; -.
DR PATRIC; fig|196627.13.peg.814; -.
DR eggNOG; COG0545; Bacteria.
DR HOGENOM; CLU_013615_12_0_11; -.
DR OMA; RVIAGWD; -.
DR BRENDA; 5.2.1.8; 960.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..118
FT /note="Probable FK506-binding protein"
FT /id="PRO_0000075353"
FT DOMAIN 33..118
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 118 AA; 12539 MW; 6E513299A181D197 CRC64;
MEKPQIELPV GPAPEDLVIS DIIVGEGAEA RPGGEVEVHY VGVDFETGEE FDSSWDRGQT
SQFPLNGLIA GWQEGIPGMK VGGRRQLTIP PEAAYGPEGS GHPLSGRTLV FIIDLISA