ID I3TUM5_TISMK Unreviewed; 296 AA.
AC I3TUM5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Parvulin-like PPIase {ECO:0000256|ARBA:ARBA00018370};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase plp {ECO:0000256|ARBA:ARBA00030642};
DE AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN Name=nifM {ECO:0000313|EMBL:AFK56463.1};
GN OrderedLocusNames=TMO_b0455 {ECO:0000313|EMBL:AFK56463.1};
OS Tistrella mobilis (strain KA081020-065).
OG Plasmid pTM2 {ECO:0000313|EMBL:AFK56463.1,
OG ECO:0000313|Proteomes:UP000005258}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK56463.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK56463.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK56463.1,
RC ECO:0000313|Proteomes:UP000005258};
RC PLASMID=Plasmid pTM2 {ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000256|ARBA:ARBA00007656}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003238; AFK56463.1; -; Genomic_DNA.
DR RefSeq; WP_014753215.1; NC_017966.1.
DR AlphaFoldDB; I3TUM5; -.
DR KEGG; tmo:TMO_b0455; -.
DR HOGENOM; CLU_034646_9_1_5; -.
DR Proteomes; UP000005258; Plasmid pTM2.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 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; PF00639; Rotamase; 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 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:AFK56463.1}; Plasmid {ECO:0000313|EMBL:AFK56463.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 138..240
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 296 AA; 31639 MW; 0569C66E0FA1E67D CRC64;
MVVIRQSPRV AAARSAAARH AHHAASHMHM ADPVPVSVDG RDIPEEEIRA EMHNHPGPDP
DTARNAAAQA LVIRELLLNA ARARDITARP GTDGQGRQEL DDEALIRALL DAEVTTPQAD
TAACRRHYDS HPGRFTTSPV WEARHILLAA TETDEAGRKA TRERAQAILA ELASDPDRFA
DLATAFSACP SRAEGGRLGQ LVRGSTVPEF EAALARMNPG EIAPAPVETR FGVHVVALDR
HLPGAVLPFE AVEARIAAWL EAASWSRGVA QFISVLAAEA DIRGVALATA EGPLVR
//
