ID A0A432ZR98_9GAMM Unreviewed; 622 AA.
AC A0A432ZR98;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=CWI84_04890 {ECO:0000313|EMBL:RUO80403.1};
OS Idiomarina tyrosinivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=1445662 {ECO:0000313|EMBL:RUO80403.1, ECO:0000313|Proteomes:UP000287996};
RN [1] {ECO:0000313|EMBL:RUO80403.1, ECO:0000313|Proteomes:UP000287996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-PW-9 {ECO:0000313|EMBL:RUO80403.1,
RC ECO:0000313|Proteomes:UP000287996};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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:RUO80403.1}.
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DR EMBL; PIQH01000004; RUO80403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432ZR98; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000287996; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:RUO80403.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000287996};
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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..366
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT COILED 277..304
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 622 AA; 69539 MW; C2C5A783598CF83B CRC64;
MMEKIREGSQ SVIVKAILVL IILTFALAGV GSYITGNSEV VVAKVNGEKI LQQDFDRAYQ
NERDRLKQQF GDMYEAIISD SGYMNQMRQN VLENLIEKAL LQQFADELGL RVSDQQVKQA
IRSMPQFKTA GSFNNDMYLM ALRNVGFTPE SFASLVREQM LQQQVMQGVA ATEFSLKPEQ
AAYYSLQNET RSGRYIVAQS ALYTSQVEVT DEELQTYYDE NSEQFYAPEQ MKVAFVELSK
ADLMNQVNVS DDEVKAFYEA NKAQYGSAEE RRVSHILVEY GDDKDAARQK IEQAQQALQQ
GEDFAAVAKQ YSTDTFSAEQ GGDLGWIEPG VMDKDFDSAV FALNNSGDVS GIVETSFGYH
IIKLTDVRES NIKPLEEVRD DIVQQLKEDK ADELFFNKQQ QLAEISFEQP DTLEPAAEAI
GVEVKNTDWF TRDSAPTVLS DQAVMNKIFA PELIDEQLNS DVITTADDKA LVVRVTDHQP
KRVKDFATVS AQIRQTLVQQ KAQDMALAQA QKWADVLASG DVPAAEVKPL ESIMRTHQQA
PRQVVQTLFT LAPQQTQAIK LNNGDAAVVQ LTDWQKGQVE DSALDSIAPR LQNRKAQVTL
AALIEQLKAE ADISRSLKAV KQ
//
