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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//