ID A0A0A5FY88_9BACI Unreviewed; 304 AA.
AC A0A0A5FY88;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=N783_21520 {ECO:0000313|EMBL:KGX83793.1};
OS Pontibacillus marinus BH030004 = DSM 16465.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385511 {ECO:0000313|EMBL:KGX83793.1, ECO:0000313|Proteomes:UP000030403};
RN [1] {ECO:0000313|EMBL:KGX83793.1, ECO:0000313|Proteomes:UP000030403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030004 {ECO:0000313|EMBL:KGX83793.1,
RC ECO:0000313|Proteomes:UP000030403};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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:KGX83793.1}.
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DR EMBL; AVPF01000082; KGX83793.1; -; Genomic_DNA.
DR RefSeq; WP_027447586.1; NZ_AVPF01000082.1.
DR AlphaFoldDB; A0A0A5FY88; -.
DR STRING; 1385511.GCA_000425225_04106; -.
DR eggNOG; COG0760; Bacteria.
DR OrthoDB; 2677468at2; -.
DR Proteomes; UP000030403; 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 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 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:UP000030403};
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 5..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 166..258
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 304 AA; 35892 MW; 00A6685EAF19DAD1 CRC64;
MTRKFLWGII VVLLITNLTT LLIWVNVRGQ VDDAENYAAK PLVENRNEPV ALVGGEPIEY
EEWEQELQNQ YGKSVLRHMI DRQVVFKMAD QYDIQIEDKL IQRELSLMET MLGVMEREQI
EAERKRWLDE VRYRFYLEEL LTKDIGIKSE KIKSYYKEHE DQYDFDETYQ FSQILVKTQQ
EANKVKKELD EGASFEMLAR EYSIDGFTKE SGGYLGYFSK KSQYLPGIYF RTAQDLSPQS
YSSPFDTDQG YVLLYVHRKL PSITFSFEEV KKQIKRELAL EYVGDSFSAK PLWEEAQVDW
VFGD
//
