ID A0A2V5JUR1_9BACL Unreviewed; 319 AA.
AC A0A2V5JUR1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=DLM86_30410 {ECO:0000313|EMBL:PYI50248.1};
OS Paenibacillus flagellatus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2211139 {ECO:0000313|EMBL:PYI50248.1, ECO:0000313|Proteomes:UP000247476};
RN [1] {ECO:0000313|EMBL:PYI50248.1, ECO:0000313|Proteomes:UP000247476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DXL2 {ECO:0000313|EMBL:PYI50248.1,
RC ECO:0000313|Proteomes:UP000247476};
RA Dai X.;
RT "Paenibacillus flagellatus sp. nov., isolated from selenium mineral soil.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000971};
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:PYI50248.1}.
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DR EMBL; QJVJ01000021; PYI50248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5JUR1; -.
DR OrthoDB; 2677468at2; -.
DR Proteomes; UP000247476; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
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; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00278}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000247476};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 174..270
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 30..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 319 AA; 35581 MW; F51E8E03742EE32C CRC64;
MRSVKVLWSV IGLLVVAVLV LTVLLVRSGD KTPEPGDASP PEPVPPGGQG GEAKKVAIIG
NRTITDEELQ QRLTDKYGAE LLGQLLDREA IRQEAEQLGM NVSRDEIEAE LKRMQEGYES
EEKFYESMKN QLGLSKAELH EDVYYKLLLE RIAVRSVQVP EADIDAYIAQ HPEEFKSYVQ
YHLLKIEVKT KEEAAKAAKD VQNGTDFASL ARKISIDPAT AKQGGDLGWV EEHDPFVPAA
LLEAARGLKT DEVSKPIALQ SGFAIIQLKE KKEVKKTVDA DTRAYIRKEL ALQRAVPLKE
LVKSLREKRH AEILLPELK
//
