ID A0A094IM07_9GAMM Unreviewed; 631 AA.
AC A0A094IM07;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=IDAT_08265 {ECO:0000313|EMBL:KFZ28725.1};
OS Pseudidiomarina atlantica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ28725.1, ECO:0000313|Proteomes:UP000053718};
RN [1] {ECO:0000313|EMBL:KFZ28725.1, ECO:0000313|Proteomes:UP000053718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ28725.1,
RC ECO:0000313|Proteomes:UP000053718};
RA Du J., Lai Q., Shao Z.;
RT "Draft genome sequence of Idiomarina sp. MCCC 1A10513.";
RL Submitted (JUN-2014) 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:KFZ28725.1}.
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DR EMBL; JPIN01000007; KFZ28725.1; -; Genomic_DNA.
DR RefSeq; WP_034732657.1; NZ_JPIN01000007.1.
DR AlphaFoldDB; A0A094IM07; -.
DR STRING; 1517416.IDAT_08265; -.
DR eggNOG; COG0760; Bacteria.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000053718; 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; 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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..366
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 631 AA; 69756 MW; D31A853EF6BB440E CRC64;
MLDRIREGSQ SLWVKVFLVL IALTFALAGI GGYIANQPEP AVAVVNGEDI TQVEFERAVE
SERNRQQQQL GDFYEQLARD PRYTQRIRAQ VVNDLINQKL LEQAARDRGL RASPEQVKAA
IRDISGFKVA GQFDNDLYLT TLRSMGYTPD GFAELIRRDL ITQQLVRGIV GSEFVLPSEV
DNTLQLLGQE RSGAFTQIAW EDYRDQVEIS DADIETWYNQ NLQNFAVPEQ VKVEYVLIDG
AELAEQLEVS EEDARAYYEG NLSRYEDAPR YRFSHILIES GDDAAAAEAE AEALLAEIEQ
GADFAELAQA NSDDIFSGEQ GGDLEWIEPG TMDADFEEAA FALENIGDIT GVVETSFGYH
IIKLTDKEEG SVTPFEEVRA EIAENLREQQ VQNRYYELQQ EVAKLAFEVP DTFSAVTEAT
GLTAQTSDWI SEGSARGALA APAVVQEVFS NEMITDRFNS DIIEISDTES VVVRVVDHKD
ATTQPLSEVT DQVRQALTVE RAQELALQRA DAIATAVRSG EATDAEFTEV SNATRQSSEY
PRMVVQTLFG MAAPAADSSN IDTVTLENGD IAVVRLDSVS AGQVDAEQSV QLQEQLLNNY
SQEVYSAVIN ALRGDAEIEM LLSSNSDSLE P
//