ID A0A1E3LR33_9SPHN Unreviewed; 639 AA.
AC A0A1E3LR33;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
DE AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN ORFNames=BFL28_06760 {ECO:0000313|EMBL:ODP36237.1};
OS Sphingomonas turrisvirgatae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1888892 {ECO:0000313|EMBL:ODP36237.1, ECO:0000313|Proteomes:UP000094487};
RN [1] {ECO:0000313|EMBL:ODP36237.1, ECO:0000313|Proteomes:UP000094487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCT13 {ECO:0000313|EMBL:ODP36237.1,
RC ECO:0000313|Proteomes:UP000094487};
RA D'Andrea M.M., Rossolini G.M., Thaller M.C.;
RT "Draft genome of the agarase producing Sphingomonas sp. MCT13.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004382}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004382}; Periplasmic side
CC {ECO:0000256|ARBA:ARBA00004382}.
CC -!- SIMILARITY: Belongs to the PpiD chaperone family.
CC {ECO:0000256|ARBA:ARBA00038408}.
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:ODP36237.1}.
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DR EMBL; MDDS01000081; ODP36237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3LR33; -.
DR STRING; 1888892.BFL28_06760; -.
DR Proteomes; UP000094487; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; PTHR47529; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D; 1.
DR PANTHER; PTHR47529:SF1; PERIPLASMIC CHAPERONE PPID; 1.
DR Pfam; PF13145; Rotamase_2; 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 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000094487};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 264..352
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 639 AA; 67056 MW; 2C7E0B304F8E8E76 CRC64;
MLFSTAGKLI ALGLLIVIAV AFALGDITNL SGGGTPAGGA LVEVGGKKVT EAELRQRLKT
AFERARQQQP TLDMTQFVNA GGFDQVLEQI VNGLALETFA RDNDMAVAKA AVDGEIASIP
AFQGLDGKFS QATFNQILAR EGITADQLRA DIARETLAQW LIGPTIGATQ VPSQFALPYA
SLLLEQRRGA VGFIPASAIA PGAAPIDAEL QGFYRRNGNR YTLPERRVVR YAVVRPEQFA
ETAKATDAEI AEAYRKNAAN YAAATRRQLA QVIVADQNAA NALAAKVKAG TGLAAAAQAI
GLKAQVIDNA DKAAFARANN AAIADAAFAA APGAVVGPIK GPIAWHVVKV EKVEQVAGKS
LEQVRGELAA EITKRKEAEL MANLRSRIDT GLADNATFDE AVADAKLTAT TSAPLFADGR
TTQDAAAQPD PLLAQIAQGG FALEQGQDPQ LIPLGEDGSF ALIKTERVFT AAPRPIAEVR
DSVTKDFIAD RQQQGARKVA AAVLADVNKG VPIADALKKT GLALPPVQPL DARRGQLAQM
GAQLPAPVRL MFSMAAKKAT LTESPNGEGY WVVWLDEIKS GNAAGNAQLI AQTRGQLGQS
LGAEYVEQFA AAVRRAVKVK RDEAAIARLK ATLSGQAGN
//
