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Database: UniProt
Entry: A4YQ79_BRASO
LinkDB: A4YQ79_BRASO
Original site: A4YQ79_BRASO 
ID   A4YQ79_BRASO            Unreviewed;       308 AA.
AC   A4YQ79;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Parvulin-like PPIase {ECO:0000256|ARBA:ARBA00018370};
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase plp {ECO:0000256|ARBA:ARBA00030642};
DE   AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN   OrderedLocusNames=BRADO2210 {ECO:0000313|EMBL:CAL76055.1};
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL76055.1, ECO:0000313|Proteomes:UP000001994};
RN   [1] {ECO:0000313|EMBL:CAL76055.1, ECO:0000313|Proteomes:UP000001994}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000256|ARBA:ARBA00007656}.
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DR   EMBL; CU234118; CAL76055.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4YQ79; -.
DR   STRING; 114615.BRADO2210; -.
DR   KEGG; bra:BRADO2210; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_1_3_5; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000001994; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF00639; Rotamase; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000313|EMBL:CAL76055.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001994};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          150..252
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   308 AA;  34035 MW;  F9745C0882A180B5 CRC64;
     MDVSSFMMRR SLAIRTHFVV ACLAASLGAT EIARAEQASA DPVIATVNGS EIHESELAMV
     DEIVGRNLPT QDRIERRDTI LKMMIDTILL SDIARERKIV DEADIARRTT FARNQGLMTQ
     LLREVGQRAV SEETVRKAYE DVVLKAASEQ TEVHLRHLVF LTKDAPDDAA RKAIEARAQA
     ALERLKKGED FAAVATETSD DPVTKSRGGD FGWRIRPELS KEYADAAFEM KNGDISPLIK
     TGVGLHIIKL EDRRTRRPPE FDTVRERVAA MVSATAQIEL VDKARAAAKI ERFDGGASIA
     PTAQPSKK
//
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