ID I3IAA5_9GAMM Unreviewed; 602 AA.
AC I3IAA5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=O59_001664 {ECO:0000313|EMBL:EIK44990.1};
OS Cellvibrio sp. BR.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK44990.1, ECO:0000313|Proteomes:UP000003395};
RN [1] {ECO:0000313|EMBL:EIK44990.1, ECO:0000313|Proteomes:UP000003395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR {ECO:0000313|EMBL:EIK44990.1,
RC ECO:0000313|Proteomes:UP000003395};
RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL Submitted (MAY-2012) 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:EIK44990.1}.
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DR EMBL; AICM01000003; EIK44990.1; -; Genomic_DNA.
DR AlphaFoldDB; I3IAA5; -.
DR STRING; 1134474.O59_001664; -.
DR PATRIC; fig|1134474.3.peg.1515; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_023843_1_1_6; -.
DR Proteomes; UP000003395; 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; IPR023058; PPIase_PpiC_CS.
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; PF13624; SurA_N_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 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:EIK44990.1}; 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 246..338
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 602 AA; 65335 MW; 9E69D97BE73D6DA0 CRC64;
MIIFALTGVE ALFNWDTSAN QAAKVNGETI TEMDVARAVG MQKQQMLNAY GDQIPAQFLS
DEYLRKPAVD NLVQRLILSQ AAKNAGMAIG DDYLAQEIAA APQFKNDAGV FDNNVYQSLL
RNMGYTHSTY TKILSEELLI NQLQAGVAVS AFSTPTQLDE LVALSFQSRD IQYVILPSGK
VRDSIELQDS EIQSYYDANQ SMFVSEEQIA VDYISLSVQD LMSSVSISEA QVRDQYEQNV
ASFVAAPERH AAHILIESND ADKVKLVGEK LSGGADFSAL AKEFSDDLGS KDQGGDLGFT
SGDAFPQEFE TALAALKVGE VSAPVKTEAG THFIKLLAEK NSTPPSFEEQ KATIEEQLKR
AEAEVSFVAQ LEKLRDISYN AESLAEVAEE LGLKVENSGL YERSKGKGIL ANPKVTEAAF
SDEVLREGNS SDVIEIDSSN VLVLKMTEHK PSQVKALADV KEQIANTLKD QKARILLTEQ
SNKFIADLNT GVSLAELSTV AGLESKEFKE ATRNTAEVDS DVLRHAFSMP KPAAGKPSVG
NLMTSSGDMA IVVVQSVSLG SVEKVTLEQK ETIGAQLASI YGRNDFSGFQ KFLKDSADIV
QK
//
