ID A0A0S3PWI0_9BRAD Unreviewed; 639 AA.
AC A0A0S3PWI0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=ppiD {ECO:0000313|EMBL:BAT60298.1};
GN ORFNames=GJW-30_1_02834 {ECO:0000313|EMBL:BAT60298.1};
OS Variibacter gotjawalensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Variibacter.
OX NCBI_TaxID=1333996 {ECO:0000313|EMBL:BAT60298.1, ECO:0000313|Proteomes:UP000236884};
RN [1] {ECO:0000313|EMBL:BAT60298.1, ECO:0000313|Proteomes:UP000236884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GJW-30 {ECO:0000313|EMBL:BAT60298.1,
RC ECO:0000313|Proteomes:UP000236884};
RA Lee J.S.;
RT "Investigation of the bacterial diversity of lava forest soil.";
RL Submitted (AUG-2015) 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}.
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DR EMBL; AP014946; BAT60298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3PWI0; -.
DR KEGG; vgo:GJW-30_1_02834; -.
DR OrthoDB; 9768393at2; -.
DR Proteomes; UP000236884; Chromosome.
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 GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; 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:BAT60298.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000236884};
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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 270..360
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 639 AA; 70627 MW; 371F957485E2589C CRC64;
MLRGIRTASS GWLGKLVMGV VVGVLAISFA IWGIGDIFRG GGRSAVASVG GTEISSEQFR
QLYTERLQQI GQQMGRPIPF NQARDLGIDR QILGQIVSET ALDEWAKRIG LGITDAEVAR
LIRSFPAFQG PDGQFDNQIF LQRLRSAGYT EARFVTEQRK LMIRQHLTES VGGTTIVPKT
YADVMNAYQN EQRSLEYVTL TAAQAGEIAD PTPEQLTTYF DSRKQLFRAP EYRRIVIVRL
SPEELAKWTT IADEDARKAY DERRARFTQA GQRQVQQIVF PSEEEARAAK KRLDEGLSFA
DLAKERGLSE TDIDLGMISR ETAQGSRFTK AMEEAFKLPE GGVSNPVQAR LGYALVRVAK
IEPDSVRPYE QVADELKQEL ARERTRNEVT TKHDKLEDER AGGANLTESA QRAGLQVTML
DGVDRSGRDA TGALVTGIPQ DVDILTPAFA AQPNTETEAL RPQAGGYVWF EVTEITPSKE
RTLDEVKDRV VARWKDDQIG ERLRAKANEM VEKLKANGTF AELAAADKLN VATAADLRRS
ARPEGLPPGA VITAFQTPKG AAASTQGQLP AERIVFKVTD IKTPPFDANS DQGKQVENLI
RTSITEDLLR QYIAYIEKEL KATVNVEALR RVSGGGVEQ
//
