FKBA_BUCAI
ID FKBA_BUCAI Reviewed; 241 AA.
AC P57599;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase FkpA;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
GN Name=fkpA; OrderedLocusNames=BU533;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
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; BA000003; BAB13226.1; -; Genomic_DNA.
DR RefSeq; NP_240340.1; NC_002528.1.
DR AlphaFoldDB; P57599; -.
DR SMR; P57599; -.
DR STRING; 107806.10039192; -.
DR EnsemblBacteria; BAB13226; BAB13226; BAB13226.
DR KEGG; buc:BU533; -.
DR PATRIC; fig|107806.10.peg.538; -.
DR eggNOG; COG0545; Bacteria.
DR HOGENOM; CLU_013615_0_2_6; -.
DR OMA; KYMSGHI; -.
DR Proteomes; UP000001806; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.10.287.460; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR000774; PPIase_FKBP_N.
DR InterPro; IPR036944; PPIase_FKBP_N_sf.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF01346; FKBP_N; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..241
FT /note="FKBP-type peptidyl-prolyl cis-trans isomerase FkpA"
FT /id="PRO_0000075364"
FT DOMAIN 153..241
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 241 AA; 26946 MW; 55D5E99740188C3F CRC64;
MILYVPKSFS ISAPISDIHL QSVLETKNTF HNNNEKLGYI LGLSFGNYVN QTFEKQKKIG
IELDRNSLLK GIQDAISGNL KLSHQDISSG LKELEKKLKH ATKIQLKKNA KENFIQGELY
MKNFSKLKGV KKTSSGLLYL LERAGEGEAL KDETKITVHY KGTLINGLEF DNSYKRGRPV
SLRLKDVILG WKEGLKYIKK GGKIKLVIPP NLAYGTEEVN GIPANSTLIF DIELLDVVNG
V