ID A0A2N3PZC5_9PROT Unreviewed; 703 AA.
AC A0A2N3PZC5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=CWS72_04140 {ECO:0000313|EMBL:PKU25762.1};
OS Telmatospirillum siberiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Telmatospirillum.
OX NCBI_TaxID=382514 {ECO:0000313|EMBL:PKU25762.1, ECO:0000313|Proteomes:UP000233293};
RN [1] {ECO:0000313|Proteomes:UP000233293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=26-4b1 {ECO:0000313|Proteomes:UP000233293};
RA Hausmann B., Pjevac P., Schreck K., Herbold C.W., Daims H., Wagner M.,
RA Pester M., Loy A.;
RT "Draft genome sequence of Telmatospirillum siberiense 26-4b1T, an
RT acidotolerant peatland alphaproteobacterium potentially involved in sulfur
RT cycling.";
RL Submitted (DEC-2017) 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:PKU25762.1}.
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DR EMBL; PIUM01000003; PKU25762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3PZC5; -.
DR Proteomes; UP000233293; 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 ECO:0000313|EMBL:PKU25762.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233293};
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 89..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 331..429
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 703 AA; 76120 MW; E2779AAE01A21268 CRC64;
MSDPAGKHLI GMRTFVRLNK LSPLREIVKV APFCAGLRKD AVKTQCAPVS FSALPSPDTP
SMMRLPSVPI PFSSRDPMLD SFRKASQSWF IKILFALLIL SFGIWGIGDV VRERADQQPA
ITVGKQTIPA AEVAEEFRRD TERLSSVFGG KLTSEQARQF GLLQRTVEQI VNRTLVDQAA
ANLGLGVDEN TLRRIIAEIP AFQNELHVFD KNVYQRALVR AGLTERQFIA MEKGDIAREQ
IGQMVASGLK APSLMADPLY RYRQESRVAE IITIPADKMP APAKPDDATL GQYHQSHSAL
FMSPELRGIT ALVVRTADVA GDIKFSDADI EKSYQIRQAE FQTPETRNIQ QVLFENAEKA
KAFAASVKQG QDFTAAAKAA GVEVSDLGWV DRKNLPLPTL ADAAFGTPGP GVAGPVESPL
GWHVLRITQV VAGKSRPLAD VKSQIVQDLV KDEATNRLYA LSTKVEDAIG SGAGVEEAAN
TLNLKPIKAT AIDEKGNGPD GKPAPGVPLI PGFLAKVFQT AQGTTTEVTQ LDDGSGYFVL
HVDNVAPPAL KPFDLVKDQV LTAWTQDQRE QAARHQAEAA AERLKNGESL AAVAGSFKVE
TTKPFLRASE EKQSVPPLLA AEMFKQQKTG GVSVVTTQGG TLVARLTQII AADPKAQPDQ
FSKARDQLSQ TLANDVMQQY LTALRADIGV HVNNGAIEAQ FQK
//