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Database: UniProt
Entry: J7LJL8_NOCAA
LinkDB: J7LJL8_NOCAA
Original site: J7LJL8_NOCAA 
ID   J7LJL8_NOCAA            Unreviewed;       222 AA.
AC   J7LJL8;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE            Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN   OrderedLocusNames=B005_0961 {ECO:0000313|EMBL:AFR11174.1};
OS   Nocardiopsis alba (strain ATCC BAA-2165 / BE74).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1205910 {ECO:0000313|EMBL:AFR11174.1, ECO:0000313|Proteomes:UP000003779};
RN   [1] {ECO:0000313|EMBL:AFR11174.1, ECO:0000313|Proteomes:UP000003779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RX   PubMed=23105086; DOI=10.1128/JB.01522-12;
RA   Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT   "Whole-Genome Sequence of Nocardiopsis alba Strain ATCC BAA-2165,
RT   Associated with Honeybees.";
RL   J. Bacteriol. 194:6358-6359(2012).
RN   [2] {ECO:0000313|Proteomes:UP000003779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RA   Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT   "Whole-genome sequence of Nocardiopsis alba strain ATCC BAA-2165 associated
RT   with honeybees.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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|RuleBase:RU363019};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; CP003788; AFR11174.1; -; Genomic_DNA.
DR   RefSeq; WP_014913626.1; NC_018524.1.
DR   AlphaFoldDB; J7LJL8; -.
DR   STRING; 1205910.B005_0961; -.
DR   KEGG; nal:B005_0961; -.
DR   PATRIC; fig|1205910.3.peg.912; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_3_11; -.
DR   OrthoDB; 9807797at2; -.
DR   Proteomes; UP000003779; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00317; cyclophilin; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:AFR11174.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003779};
KW   Rotamase {ECO:0000256|RuleBase:RU363019};
KW   Signal {ECO:0000256|RuleBase:RU363019}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU363019"
FT   CHAIN           21..222
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /evidence="ECO:0000256|RuleBase:RU363019"
FT                   /id="PRO_5039759734"
FT   DOMAIN          54..218
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          24..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   222 AA;  23276 MW;  20C193ADDB0A31C2 CRC64;
     MNRLTLPVSI LACTALFATA ACGSSENDSD AAPDAETPTA PEESPLPAEV DIDGVEGAVL
     HTSAGDIEVE LYPEEAPITV ANFVGLAEGD LATNPETGAD EFYDGTIFHR VIQDFMVQGG
     DPQGSGRGGP GYQFQDEFES GLTFDDPGIL AMANSGPGTN GSQFFITVAP TPHLNNMHTI
     FGKVADEESL EIVNEISTVE TDGNDRPTDD IVLESITVQR AG
//
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