ID A0A418WBL1_9PROT Unreviewed; 638 AA.
AC A0A418WBL1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=D3874_10625 {ECO:0000313|EMBL:RJF87421.1};
OS Oleomonas cavernae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Oleomonas.
OX NCBI_TaxID=2320859 {ECO:0000313|EMBL:RJF87421.1, ECO:0000313|Proteomes:UP000284605};
RN [1] {ECO:0000313|EMBL:RJF87421.1, ECO:0000313|Proteomes:UP000284605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1W22B-8 {ECO:0000313|EMBL:RJF87421.1,
RC ECO:0000313|Proteomes:UP000284605};
RA Zhu H.;
RL Submitted (SEP-2018) 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:RJF87421.1}.
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DR EMBL; QYUK01000011; RJF87421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418WBL1; -.
DR OrthoDB; 9768393at2; -.
DR Proteomes; UP000284605; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000284605};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..355
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 638 AA; 66721 MW; 222EEAD1D19CD3CA CRC64;
MLQTLRKGAS TWVVRIFLGI LMVSFGIGIW QGNTLFSSAA DTTVATVGDT EISSQAFTVA
LDREVRRLQQ QLGAGFTREQ ALAFNVQGGV LSQLLSDATV AEAARSFGLR VPDELVAREI
AAIPAFQDFT GKFDAARFQA VLRQAQMTEA TLTQQIRAEL VRAQLYGPAA GGARTPTIVA
QTLYAHRNER RVIDYFTLAP AALGPIPQPD EAAIDAYYKA NPQAFTAPEF RAITLLIADP
AEIAKTTAPT EDAIAAAYEE RKGEFGTPEK REIVQMVLKT QAEADTAVSK LNSGGDFVAV
AKELANLSEA DTKLGTVTKG TLPAALDEAA FAAAEGAIGG PVETPLGWHV FKVVKVEAAS
VKPMAEVHDT LRDALALDAA QSQITQIQKS LQDELAGGAS LEDAGQRLNL SVRKVAAVDA
GGKDEAGKPV EGLPEAPPLL PGLFQAATGR NGDMIDTDGG GFVIGRVDTI SPAALRPLDQ
VRGQVIAGWQ AAETQDRLGK LAAETVKGIN DGKDIAAAAK AAGATPGTVG PGLRSGDAIF
VALPPALVTA LFEVDKGKAA SAPAADETGI IIGAVRGIEA ADPAADAEGV KKLAETLRED
FAGDLAGVFE ADLRARFGIS IHEQTYNSLI GQRGRSEQ
//