ID B6BI41_SULGG Unreviewed; 92 AA.
AC B6BI41; H1FV00;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase C {ECO:0000256|ARBA:ARBA00040926};
DE AltName: Full=Parvulin {ECO:0000256|ARBA:ARBA00043072};
DE AltName: Full=Rotamase C {ECO:0000256|ARBA:ARBA00041926};
GN Name=ppiC {ECO:0000313|EMBL:EHP30194.1};
GN ORFNames=SMGD1_1670 {ECO:0000313|EMBL:EHP30194.1};
OS Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP30194.1, ECO:0000313|Proteomes:UP000006431};
RN [1] {ECO:0000313|EMBL:EHP30194.1, ECO:0000313|Proteomes:UP000006431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD1 {ECO:0000313|EMBL:EHP30194.1,
RC ECO:0000313|Proteomes:UP000006431};
RX PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA Labrenz M., Jurgens K.;
RT "Genome and physiology of a model Epsilonproteobacterium responsible for
RT sulfide detoxification in marine oxygen depletion zones.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000256|ARBA:ARBA00007656}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHP30194.1}.
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DR EMBL; AFRZ01000001; EHP30194.1; -; Genomic_DNA.
DR RefSeq; WP_008335405.1; NZ_DS995286.1.
DR AlphaFoldDB; B6BI41; -.
DR STRING; 929558.SMGD1_1670; -.
DR PATRIC; fig|929558.5.peg.1661; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_090028_6_1_7; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000006431; Unassembled WGS sequence.
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 PANTHER; PTHR43629; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR43629:SF2; RHODANESE-LIKE/PPIC DOMAIN-CONTAINING PROTEIN 12, CHLOROPLASTIC; 1.
DR Pfam; PF00639; Rotamase; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:EHP30194.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006431};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278}.
FT DOMAIN 1..90
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 92 AA; 9692 MW; 068135FF9C1FD812 CRC64;
MAYATARHIL VASEDECNTL KAEIENGASF ESVAQAHSQC PSGAQGGDLG QFGPGQMVPE
FDKAVFSGDV GVLYGPIQTQ FGYHLLEVTS RG
//