ID A0A0Q7JNL1_9BACL Unreviewed; 369 AA.
AC A0A0Q7JNL1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:KQX57740.1};
GN ORFNames=ASD40_32280 {ECO:0000313|EMBL:KQX57740.1};
OS Paenibacillus sp. Root444D2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736538 {ECO:0000313|EMBL:KQX57740.1, ECO:0000313|Proteomes:UP000051657};
RN [1] {ECO:0000313|EMBL:KQX57740.1, ECO:0000313|Proteomes:UP000051657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root444D2 {ECO:0000313|EMBL:KQX57740.1,
RC ECO:0000313|Proteomes:UP000051657};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX57740.1, ECO:0000313|Proteomes:UP000051657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root444D2 {ECO:0000313|EMBL:KQX57740.1,
RC ECO:0000313|Proteomes:UP000051657};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQX57740.1}.
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; LMEO01000021; KQX57740.1; -; Genomic_DNA.
DR RefSeq; WP_057303826.1; NZ_LMEO01000021.1.
DR AlphaFoldDB; A0A0Q7JNL1; -.
DR STRING; 1736538.ASD40_32280; -.
DR Proteomes; UP000051657; 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.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00278}; Reference proteome {ECO:0000313|Proteomes:UP000051657};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..369
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039155630"
FT DOMAIN 201..301
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 330..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 39864 MW; 6FE25EEF681644BE CRC64;
MLPNDTSKQR RFSKKWILSM VALLLAFSVL SACGSKKEGA ATASPSPAST AAATGNPSDV
IATYKEGGKI TRGEFNSFIS VNKMFSPQLA QFMTDPAFQQ DMLKQMVTFR VLSAKADDKV
KADADKQVTE QMKAITDYFG KQEGGMDKQL KDNGIELKDI ESLMKMSFYT MGSMESKITD
QAVQDSYKEQ AATHAFDIAT VSHILISLKD AATQKDLRTK DEALARAKEV KGKLDKGGDF
AALAKEYSDD PGSKEAGGTY KDADINQWVP EFKQAASTLP LNTISDPVES SFGYHVMKVE
SRSTKPLDDT LKTQIKSQLA EKSLSEFAEK EYPNLIQTNN LPKPEASPAP AASPAASPAA
SPAASPAAK
//
