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Database: UniProt
Entry: A0A268S6W3_9BACL
LinkDB: A0A268S6W3_9BACL
Original site: A0A268S6W3_9BACL 
ID   A0A268S6W3_9BACL        Unreviewed;       388 AA.
AC   A0A268S6W3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:PAF28318.1};
GN   ORFNames=CHI14_28390 {ECO:0000313|EMBL:PAF28318.1};
OS   Paenibacillus sp. 7516.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2022549 {ECO:0000313|EMBL:PAF28318.1, ECO:0000313|Proteomes:UP000216732};
RN   [1] {ECO:0000313|EMBL:PAF28318.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7516 {ECO:0000313|EMBL:PAF28318.1};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAF28318.1}.
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DR   EMBL; NPBI01000046; PAF28318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268S6W3; -.
DR   Proteomes; UP000216732; Unassembled WGS sequence.
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}; Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..388
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038578371"
FT   DOMAIN          176..280
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   REGION          320..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  42797 MW;  18444CC05E7D3437 CRC64;
     MLPKYKKVGK VLSVSMVAVL SLSLLAACGK KDEAAAPETN DTSAVVATYD GGTITANEFD
     MEQRVMKFLY PEYAQMMEMD DFKDYLVRQE VAYEYLSGKA SEEAKTEGAK VATEQFDKMK
     ASVQADQWTE MLKAQNLTDQ NIKDYMTRIM TVIKDKETGV TEDAIKKEFE TNKDQFTTAS
     VRHVLINFTD PDTQKERKKE DALKIAKEVK TKLDAGEDFA KVAKEYSEDP GSADNGGLYE
     NTPVSNWVEA FKEAAKTLPL NKISDPVETE YGYHVMKVES RTEADYSKLT DEQKETLKSQ
     LAAAEIDTFM TNELDKIVKE VNLPKTDKAE EGTTEGTEGT TGTGTGTEGD KSTETKTDES
     TGTDAKTDQG TKTESDATTG DSADTSSK
//
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