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Database: UniProt
Entry: E3EDW6_PAEPS
LinkDB: E3EDW6_PAEPS
Original site: E3EDW6_PAEPS 
ID   E3EDW6_PAEPS            Unreviewed;       372 AA.
AC   E3EDW6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:ADO54032.1};
GN   Name=prsA1 {ECO:0000313|EMBL:ADO54032.1};
GN   ORFNames=PPSC2_00215 {ECO:0000313|EMBL:ADO54032.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO54032.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO54032.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO54032.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(2011).
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DR   EMBL; CP002213; ADO54032.1; -; Genomic_DNA.
DR   RefSeq; WP_013368680.1; NC_014622.2.
DR   AlphaFoldDB; E3EDW6; -.
DR   STRING; 1406.LK13_13230; -.
DR   KEGG; ppm:PPSC2_00215; -.
DR   PATRIC; fig|886882.15.peg.42; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_5_1_9; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000006868; 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; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   PANTHER; PTHR47245:SF2; SLR0208 PROTEIN; 1.
DR   Pfam; PF13616; Rotamase_3; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW   ProRule:PRU00278}; Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..372
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039504519"
FT   DOMAIN          179..283
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   REGION          328..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   372 AA;  40932 MW;  1F69A54B61473859 CRC64;
     MSQLNKRKPW RMLSLGMAAL LAISVLAACT KQADENKVKD EPKDNSKVVV TYKGGTITEN
     EFNQEISMMK FLYPEYEAAL ASDQVREQIV KQEVVYKLLA AKADDKAKEE GAKQGNEQLE
     QYKKSVGEDK FKTFLSDQKL TEQGVKDYFT RVMTVINSET NKVTDDQLKQ EFEKNKDQFT
     TATVRHVLIN FEDPKTKKQR TKEATLKLAK EVKAKLDGGA DFATIAKKYS EDPGSASNGG
     LYENASVAQW VPAFKEAAET QPINKIGEPV ETEYGYHVIK VESRNEPTFD KLKDNEKAAL
     KNKLAGESIQ NFTENDLTKL DLKINLPKAP ATQEKSGATS GAGSTTTPSG TTSGTGDSKA
     GTTKDGAANE GK
//
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