ID A0A239ADR9_9PROT Unreviewed; 629 AA.
AC A0A239ADR9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN05880556_101655 {ECO:0000313|EMBL:SNR93806.1};
OS Azospirillum sp. RU38E.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=1907313 {ECO:0000313|EMBL:SNR93806.1, ECO:0000313|Proteomes:UP000198368};
RN [1] {ECO:0000313|EMBL:SNR93806.1, ECO:0000313|Proteomes:UP000198368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU38E {ECO:0000313|EMBL:SNR93806.1,
RC ECO:0000313|Proteomes:UP000198368};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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}.
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DR EMBL; FZOI01000001; SNR93806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239ADR9; -.
DR OrthoDB; 9768393at2; -.
DR Proteomes; UP000198368; 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; 2.
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:SNR93806.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198368};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..349
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 629 AA; 67282 MW; 61671184898709F6 CRC64;
MLQIIRSTAG SWVVKILFVV LIISFAVWGI GDITRGVQTG VAKVGDTNIT PQELDREFKA
EINRLRQVMG PDFDEAKARQ LGLVDRALEQ LIQRTLLLKA AEDAGIRIAD QTVVDMVSKV
PAFKNGLGQF DPALMRALLA QNGYTEHGFA EQVRADLAQG DIAGAITAGT TVPRALAEQL
FRYREEARRF DLVTIPNTAM PDAPAPEEAV LAQFHQDKAV RYTAPEYRDL TIGLIEASAL
AKEIQVSDEQ RQEYYDAHQA DYVTAERRTL TQIVFPDKAA ADKALAAIQG GKTLEQVAKD
AKQEAVKLDD VLKADLPAEL AEPVFTAEQG KPVGPVESAF GFHVALVSTI KAGGTRTLAE
VKDEVTAKVR QEKSIDKLYE ASTKLEDALA NGTPVADAVK EFGGRTIKLD GVDNQGKDKK
GVAKTDGLPT ADAILTNAFS LPEGQNGSVA EAGSDAFYVV HVDAVTPSAV KPLAEVKGQV
LADWQAEQKA ATAKKKAEEV AEKLRAGATP KDAAAGITGA LVQRSEPMRR AGGPNLSLPA
SLFEPMFAAK PDTVAVGASS SGQVVAKLVE IIPADPSLVQ AATAINMLSS NMAEAMASDL
MLQYLAGLRA RYGVTINRSV IDTMYRPQE
//