ID A0A1G2B452_9BACT Unreviewed; 385 AA.
AC A0A1G2B452;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=PpiC domain-containing protein {ECO:0000259|PROSITE:PS50198};
GN ORFNames=A3F54_05345 {ECO:0000313|EMBL:OGY83775.1};
OS Candidatus Kerfeldbacteria bacterium RIFCSPHIGHO2_12_FULL_48_17.
OC Bacteria; Candidatus Kerfeldbacteria.
OX NCBI_TaxID=1798542 {ECO:0000313|EMBL:OGY83775.1, ECO:0000313|Proteomes:UP000176952};
RN [1] {ECO:0000313|EMBL:OGY83775.1, ECO:0000313|Proteomes:UP000176952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGY83775.1}.
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DR EMBL; MHKD01000019; OGY83775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2B452; -.
DR STRING; 1798542.A3F54_05345; -.
DR Proteomes; UP000176952; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR47245:SF2; SLR0208 PROTEIN; 1.
DR Pfam; PF13616; Rotamase_3; 1.
DR Pfam; PF13624; SurA_N_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 207..341
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 385 AA; 41591 MW; 1D351CE0F71DA878 CRC64;
MTEQTQGKEN KKDEGADKVP AAAVTGKDPE TAEKKDASLG GADRVGSAKR GISLERLRNW
WAPVILVLAV VFFGGTALAV YSFDMNNGFT RAVTGVFPFP AAMVNGKIVN YHDYQEQVDA
LKYYNDKQVE LGLPAITFEE GQTLEDAALQ RLVETRLTLD EAKKYGVEVT DEEIDSAFTD
FVAAQGGNTD EVVKSLRDYY NWSVDQFKDT FIRDVLYRQD VTKGLVADAQ FDVEKRKEAE
AVLARVQKAV DAAAVVPAEG GDAADGADAA AEGAATPETF ESIAKEVSDD PTSAENGGDL
GVFTLQQMVP EFANAVAGLE VGKVSGVVHT EFGFHIVRLD KVIPGESGDP TQDQYAAHHI
LIAGTSLDDY LKAREAAAKI RRFVP
//
