ID A0A0K9F872_9BACI Unreviewed; 323 AA.
AC A0A0K9F872;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=ACZ11_15090 {ECO:0000313|EMBL:KMY30710.1};
OS Lysinibacillus xylanilyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=582475 {ECO:0000313|EMBL:KMY30710.1, ECO:0000313|Proteomes:UP000037326};
RN [1] {ECO:0000313|Proteomes:UP000037326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23493 {ECO:0000313|Proteomes:UP000037326};
RG Consortium for Microbial Forensics and Genomics (microFORGE);
RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA Blagden T., Winegar R.A.;
RL Submitted (JUL-2015) 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:KMY30710.1}.
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DR EMBL; LFXJ01000007; KMY30710.1; -; Genomic_DNA.
DR RefSeq; WP_049667381.1; NZ_LFXJ01000007.1.
DR AlphaFoldDB; A0A0K9F872; -.
DR PATRIC; fig|582475.4.peg.2519; -.
DR OrthoDB; 2677468at2; -.
DR Proteomes; UP000037326; 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; PF13145; Rotamase_2; 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 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 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 179..271
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 323 AA; 36672 MW; 73439B24D5E994B3 CRC64;
MSSTRNRRPL SAATPNQTPL LQRRLKTKPA LTVIAILLLG NILWFISWLI PNKDLEIGSD
EQVAAVDGDT ITRQEWMVAM EERYGKETLQ NLVNESVMEK AAKKFKIQVT DKEIDLELAL
MRSAQDKFDT AMQNLSSEQL RQKIRSQLIL DKVLTKDMVI KEDSIEKYYE ENQALYNTKT
SYRTNFIEVD SKKAAEEALK ELKDPSDFSV LAREISVDSA SASLGGDIGF LTEKQENVDP
AILKAVNELK AGEVSKAFKL ANGHYGIVQV QEITEGQSFT YDDVKEHIER ELALEQLPQH
VTPETFWSEF NATWYYGEAK KGK
//
