ID A0A2S6NNK3_RHOGL Unreviewed; 374 AA.
AC A0A2S6NNK3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=CCS01_01840 {ECO:0000313|EMBL:PPQ38828.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ38828.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ38828.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ38828.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
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:PPQ38828.1}.
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DR EMBL; NHRY01000037; PPQ38828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6NNK3; -.
DR Proteomes; UP000239724; Unassembled WGS sequence.
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; 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; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Reference proteome {ECO:0000313|Proteomes:UP000239724};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 223..314
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 353..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 40574 MW; 9DCCD5A1BE46085B CRC64;
MPPFTISCAR NCSPRRYGSR SGRPGPSSTY AGSTWTDRLW IPVPGSRAAP APRRRTEPAL
VTRARFRHKR ARHSSGVAMK RFPDCSFGAP ARWLAVAALC CAVSAGAAVA DTKPDPVLAT
VNGQPIHLSD VRDAVGSLPP QARAMPPQQL YPMLLEQLID ARALLIQAQR TGLDKDPDVQ
KSMQMAADHA LETALLSKVV RPQITDEAVK AKYEQDIAKK PGEIEVHARH ILVPDEATAK
KIIAELKKGA DFAALSKQYS KDPGAAQQGG DLGFFKKSEM VPEFADVAFS LKDGEIAPNP
VKTQFGWHVI QVLGHRTAPP PSFAEQRDQL RQAMIQAAVQ KEVASVRSAV KIEKFNPDGT
PVKPTDTAEP PPEK
//
