ID F9ZU23_ACICS Unreviewed; 258 AA.
AC F9ZU23;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase ppiD {ECO:0000313|EMBL:AEK59319.1};
GN OrderedLocusNames=Atc_2672 {ECO:0000313|EMBL:AEK59319.1};
OS Acidithiobacillus caldus (strain SM-1).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK59319.1, ECO:0000313|Proteomes:UP000006135};
RN [1] {ECO:0000313|EMBL:AEK59319.1, ECO:0000313|Proteomes:UP000006135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK59319.1,
RC ECO:0000313|Proteomes:UP000006135};
RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT "Unraveling the Acidithiobacillus caldus complete genome and its central
RT metabolisms for carbon assimilation.";
RL J. Genet. Genomics 38:243-252(2011).
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000256|ARBA:ARBA00007656}.
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DR EMBL; CP002573; AEK59319.1; -; Genomic_DNA.
DR RefSeq; WP_004869166.1; NC_015850.1.
DR AlphaFoldDB; F9ZU23; -.
DR STRING; 990288.Atc_2672; -.
DR GeneID; 69613111; -.
DR KEGG; acu:Atc_2672; -.
DR HOGENOM; CLU_034646_1_1_6; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000006135; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.1040; -; 1.
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; PF13616; Rotamase_3; 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:AEK59319.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006135};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..258
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007914463"
FT DOMAIN 126..216
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 258 AA; 28116 MW; 34EE09F92182A91D CRC64;
MKLRSIVLAA LVGTFAAPVF AAPVATVNGQ AIDNSQVQAI LSMSPELAKE PNAREQVVQN
LVNMEVLSQY AMKHNLDQSA DVKERLALAK RQILADAAVD QYIKEHPVPE SEIQAAYNKF
VAAMGKKEYE VRHILVKTKA EADKILAELK AGKKFSTLAE KYSIDKASAA HGGELGWIVP
GMVVPPFAEA IEKAPIDKPV GPVQTQFGYH IIEVQATKPL TPPPLSAMKD RIKAQLQQEE
AAKFVSDLRS QAKIDITK
//
