ID U5NA99_9BURK Unreviewed; 261 AA.
AC U5NA99;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase C {ECO:0000313|EMBL:AGX87114.1};
GN Name=ppiC {ECO:0000313|EMBL:AGX87114.1};
GN ORFNames=Cenrod_1016 {ECO:0000313|EMBL:AGX87114.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX87114.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX87114.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX87114.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000256|ARBA:ARBA00007656}.
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DR EMBL; CP004885; AGX87114.1; -; Genomic_DNA.
DR RefSeq; WP_022771933.1; NC_022576.1.
DR AlphaFoldDB; U5NA99; -.
DR STRING; 946483.Cenrod_1016; -.
DR KEGG; cbx:Cenrod_1016; -.
DR PATRIC; fig|946483.4.peg.1023; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_1_1_4; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000017184; 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:AGX87114.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017184};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..261
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007930733"
FT DOMAIN 131..222
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 261 AA; 28981 MW; 31F5FCBB5796C320 CRC64;
MKMKFVAAAV AAVVLGSLHS VAWSQNVAVV NGKAVPKAKV DALSQQIARS GREITPDIEK
QIKDEVIVRE IFMQEAQRQG LDATEDFQTQ IELAKQNILI RELFASYQKA HPATEEEIKA
EYDQFVASNS GKEYKARHIL VETEEQAKSI LAQLKKGAKF DELAKKSSKD PGSAARGGDL
GWSPAGNYVA EFSQAMTKLG KGKTSDAPVK SQFGYHIIRV DDVRDAQLPK LEDIKPQVVQ
RLMQRKLSKY QDELRAKAKI E
//
