ID A0A0D6TLD0_9FLAO Unreviewed; 700 AA.
AC A0A0D6TLD0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=SY27_09430 {ECO:0000313|EMBL:KIX20991.1};
OS Flavobacterium sp. 316.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1603293 {ECO:0000313|EMBL:KIX20991.1, ECO:0000313|Proteomes:UP000032747};
RN [1] {ECO:0000313|EMBL:KIX20991.1, ECO:0000313|Proteomes:UP000032747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=316 {ECO:0000313|EMBL:KIX20991.1,
RC ECO:0000313|Proteomes:UP000032747};
RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT Genomic and a Proteomic Perspective.";
RL Submitted (FEB-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}.
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:KIX20991.1}.
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DR EMBL; JYGZ01000004; KIX20991.1; -; Genomic_DNA.
DR RefSeq; WP_045969576.1; NZ_JYGZ01000004.1.
DR AlphaFoldDB; A0A0D6TLD0; -.
DR STRING; 1603293.SY27_09430; -.
DR PATRIC; fig|1603293.4.peg.1953; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000032747; 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 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; PF13616; Rotamase_3; 1.
DR Pfam; PF13623; SurA_N_2; 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:KIX20991.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000032747};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 346..451
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 700 AA; 77061 MW; 8884747EAB9736C5 CRC64;
MAVLSKIRQR SFFLIVIIAL ALFSFVLADV IKNGSFGSDS SNVGSVDGTD IVAQQFMQKV
AQVEKQSQQQ GQNMSSTQAM NSVWEQEVRS VLVGKEIEKI GLGIGNEQVI NVVKTNPYFS
QNPQFLNDAG KFDENKFKEF VKSIKNDPNQ DRWVQWKQFE EDVAKSAVEQ LYYNMIKGGV
YTTKAEGKFK HELDNKKIDF DYVTVGFSTI NDDQVKVSDD EIMAYMKKNP KKYKSDDTRT
IDYVFIENKP SEQDEKDLET KFYGYVNGVA NGKDSIPSFK DVKNENVIAF VNKESEIPFD
STYVTKKDLP IDSQEQLFNL STGEVFGPYV NNEYQSLSRL MGRKSNASAK ASHILLAYEG
AQNSSATRTK EEAQALANSL MAQAKSNPAN FAMLASTNSD DPGSKNNGGE YDNITPGQMV
PTFNDFVFNN PVGAIGVVET DYGFHVIKVS AKYDAVQLAT ISQKIEPSST TIDAIYNKAS
KFEADANEKS FEEVAKASKL TIVPASNIKP SDEFIQGLGA QREIVRWSFN EDTEIGTIKR
FETPKGYVIA TLKSKNDSGL LAMDVAKESV GVILRNEKKA ELIKKKMSGS SLEDVAKVSG
GSVLSATNVS LGTPVIQNVG SESKVVGTAF SLAEGKTSKL IVGNTGVFMV KAKKVVAAPA
VDNFTSFITQ EKSQQASSSQ IRAYQAIKEK SKIKDNRANF
//
