(data stored in ACNUC7421 zone)

SWISSPROT: A8FQI5_SHESH

ID   A8FQI5_SHESH            Unreviewed;       263 AA.
AC   A8FQI5;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 68.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   OrderedLocusNames=Ssed_0495 {ECO:0000313|EMBL:ABV35108.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35108.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35108.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35108.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV35108.1; -; Genomic_DNA.
DR   RefSeq; WP_012140845.1; NC_009831.1.
DR   ProteinModelPortal; A8FQI5; -.
DR   STRING; 425104.Ssed_0495; -.
DR   EnsemblBacteria; ABV35108; ABV35108; Ssed_0495.
DR   KEGG; sse:Ssed_0495; -.
DR   eggNOG; ENOG4108V1T; Bacteria.
DR   eggNOG; COG0545; LUCA.
DR   HOGENOM; HOG000154888; -.
DR   KO; K03772; -.
DR   OMA; LAYGNEF; -.
DR   OrthoDB; POG091H05SW; -.
DR   BioCyc; SSED425104:GH7Q-517-MONOMER; -.
DR   Proteomes; UP000002015; 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   Gene3D; 1.10.287.460; -; 1.
DR   InterPro; IPR023566; PPIase_FKBP.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR000774; PPIase_FKBP_N.
DR   PANTHER; PTHR43811; PTHR43811; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF01346; FKBP_N; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQI5.
DR   SWISS-2DPAGE; A8FQI5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915, ECO:0000313|EMBL:ABV35108.1};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    263       Peptidyl-prolyl cis-trans isomerase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002721327.
FT   DOMAIN      152    237       PPIase FKBP-type. {ECO:0000259|PROSITE:
FT                                PS50059}.
SQ   SEQUENCE   263 AA;  28485 MW;  14D0F9C0F9E921F7 CRC64;
     MKKFTKSSLA VITGLSLFVS GYSIADDDTS SDVQQQSYSI GASLGKYVSS QIYSQKQLGA
     EVDVDLVVKG VIDALKGEQK YSDEEILTFL NQRAEQLNAA REAEDARIAL KNMTEGSAYL
     ASNKKSDKVT VTESGLQYEV ITMGEGRKAN PEDVVTVHYK GLLIDGTEFD NSYERDEPNR
     FALMSVIEGW QEGIPLMPEG STFKFTIPSE LAYGKKQVGI IPPSSILVFE VELVKVEEPG
     ENSHGMGLSG MGMGGMMGGG KAH
//

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