ID V6S4V4_9FLAO Unreviewed; 700 AA.
AC V6S4V4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=IP98_02216 {ECO:0000313|EMBL:TWI10406.1};
OS Flavobacterium cauense R2A-7.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1341154 {ECO:0000313|EMBL:TWI10406.1, ECO:0000313|Proteomes:UP000319848};
RN [1] {ECO:0000313|EMBL:TWI10406.1, ECO:0000313|Proteomes:UP000319848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7270 {ECO:0000313|EMBL:TWI10406.1,
RC ECO:0000313|Proteomes:UP000319848};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
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:TWI10406.1}.
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DR EMBL; VLKQ01000010; TWI10406.1; -; Genomic_DNA.
DR RefSeq; WP_023569305.1; NZ_VLKQ01000010.1.
DR AlphaFoldDB; V6S4V4; -.
DR STRING; 1341154.FCR2A7T_01100; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000319848; 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:TWI10406.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 345..451
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 700 AA; 76182 MW; 1FD90743211E9D8C CRC64;
MAVLSKIRQR SILLIGVIGF CLLAFVVGDV IQNGGFNQTS RNVGSVNGED ISAQDFLQKV
SAAEKNGQGV SGTQAANGVW EQEVKKILLN GEFEKLGLKI GKDQLINVIK QNPNIAQNPQ
FLNAAGVFDV NKFNEFLATL KNSDSERWNA WLKDEQNIQD FALEQMYYTM IKSGLVTTKV
EAKAAYAKEN DKVDFDYVTV AYSTIKDDQV KVSDAEIMDY MKKNEKKYKS ENSRDIEFVF
IENKPSVEDE AEMKTTINGL LSGRVVYNDK TGKNDTLPGF KAAANVEEFV NANSDIKFDS
TYIAKKDLPL ENQEQLFNLP QGEVFGPYIY NGYYCLSKML GRQAGSTAKA SHILLSYTGS
KAPAAAKRTK EEAKAKAEEL LAQVKANPAS FPMLAMVNTD DTGSKQNGGS YDNITKGQMV
KPFNDYLFNN PVGSIGIVET EFGYHVIKVD AKYDAVRLAT IARKIEPSET TADQIYTKAT
KFEADANEKD FATVAKEANL TVNPATVKGT DEYLPAVGSQ RGVVTWAFNK GTKIGDVKKF
DNLQGHIIAR LKATNESGLM SVEQARGAVE PILKNKKKAE LIKAKMTGTT LEAVAQKSGA
SIIPAAGIAL EGASIPNVGS EPKVVGKAFG LGAGKTSKLI DGEMGVYMIR TKAVVKAPAL
PNYTAYVTKL KSQNQGTASG RVITALKSAA DIEDNRVEFQ
//
