ID J5PIY3_9RHOB Unreviewed; 342 AA.
AC J5PIY3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=A33M_3723 {ECO:0000313|EMBL:EJW10982.1};
OS Rhodovulum sp. PH10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW10982.1, ECO:0000313|Proteomes:UP000002930};
RN [1] {ECO:0000313|EMBL:EJW10982.1, ECO:0000313|Proteomes:UP000002930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH10 {ECO:0000313|EMBL:EJW10982.1,
RC ECO:0000313|Proteomes:UP000002930};
RX PubMed=23105089; DOI=10.1128/JB.01695-12;
RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT India.";
RL J. Bacteriol. 194:6363-6363(2012).
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:EJW10982.1}.
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DR EMBL; AKZI01000079; EJW10982.1; -; Genomic_DNA.
DR RefSeq; WP_008387935.1; NZ_AKZI01000079.1.
DR AlphaFoldDB; J5PIY3; -.
DR STRING; 1187851.A33M_3723; -.
DR PATRIC; fig|1187851.3.peg.2816; -.
DR eggNOG; COG0760; Bacteria.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000002930; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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 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:UP000002930};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..342
FT /note="Parvulin-like PPIase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003784320"
FT DOMAIN 160..262
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 301..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 36498 MW; 5A8BCD222A04FC0C CRC64;
MITLASSRPA RARVGFVAAL LAAVLVPAGG VALAQAQSPA APAAQATAPA GDPVVATVDG
TPIRQSDLAQ AEKDVGAAIP AGTEEAKRDW LVNYMTDMTL LAKQAEADKI ADAPEFKARL
AYLRQKALME AVLDKTGAEA TSDEAMRHVY QEALKQMGDE QEVHARHILF RVPDAGDAEA
AKKAEEAAKA ALARIKKGED FAKVAKELTD DPPGKQDGGD LGWFTKEQMV PPFSEAAFKL
EEGQVSEPVK TSFGWHIIKV EGKRKRQPPT FEQVKEQIET FVTRKAQIDL VNKLRNDAKI
VRLDKPADAA KPDAAKPDAA KSDAGKADAA KPDAGKPAPE KK
//
