(data stored in SCRATCH zone)

SWISSPROT: B8I9L2_METNO

ID   B8I9L2_METNO            Unreviewed;       140 AA.
AC   B8I9L2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   OrderedLocusNames=Mnod_0221 {ECO:0000313|EMBL:ACL55265.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55265.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55265.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0). {ECO:0000256|RuleBase:RU003915}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC       {ECO:0000256|RuleBase:RU003915}.
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DR   EMBL; CP001349; ACL55265.1; -; Genomic_DNA.
DR   RefSeq; WP_015926978.1; NC_011894.1.
DR   ProteinModelPortal; B8I9L2; -.
DR   STRING; 460265.Mnod_0221; -.
DR   EnsemblBacteria; ACL55265; ACL55265; Mnod_0221.
DR   KEGG; mno:Mnod_0221; -.
DR   eggNOG; ENOG4108V1T; Bacteria.
DR   eggNOG; COG0545; LUCA.
DR   HOGENOM; HOG000154887; -.
DR   KO; K01802; -.
DR   OMA; RVIAGWD; -.
DR   OrthoDB; POG091H05SW; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   InterPro; IPR023566; PPIase_FKBP.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR43811; PTHR43811; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B8I9L2.
DR   SWISS-2DPAGE; B8I9L2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915, ECO:0000313|EMBL:ACL55265.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    140       Peptidyl-prolyl cis-trans isomerase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002874206.
FT   DOMAIN       48    140       PPIase FKBP-type. {ECO:0000259|PROSITE:
FT                                PS50059}.
SQ   SEQUENCE   140 AA;  14532 MW;  6598EE5F3A747801 CRC64;
     MRLSPFLRAG ALLIAMTAAA SSADFTTTPS GLKYKDDVVG TGPAPAAGQT VSVHYTGWLD
     EKGRKGKKFD SSVDRGQPLN FAVGTGQVIK GWDEGLSTMK VGGKRTLVIP PDLGYGARGA
     GGVIPPNATL IFDVELLGVR
//

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