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Database: UniProt
Entry: A0A437PMD5_9BACT
LinkDB: A0A437PMD5_9BACT
Original site: A0A437PMD5_9BACT 
ID   A0A437PMD5_9BACT        Unreviewed;       705 AA.
AC   A0A437PMD5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE   AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN   ORFNames=EOJ36_10180 {ECO:0000313|EMBL:RVU23440.1};
OS   Sandaracinomonas limnophila.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Sandaracinomonas.
OX   NCBI_TaxID=1862386 {ECO:0000313|EMBL:RVU23440.1, ECO:0000313|Proteomes:UP000282832};
RN   [1] {ECO:0000313|EMBL:RVU23440.1, ECO:0000313|Proteomes:UP000282832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSY-15 {ECO:0000313|EMBL:RVU23440.1,
RC   ECO:0000313|Proteomes:UP000282832};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) 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:RVU23440.1}.
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DR   EMBL; SACY01000005; RVU23440.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437PMD5; -.
DR   OrthoDB; 9812372at2; -.
DR   Proteomes; UP000282832; 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:RVU23440.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282832};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          346..445
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   705 AA;  77850 MW;  2B102C0F70C3C7EE CRC64;
     MALITKIREK SGLAAAAIAI SLILFLVGSD IFQGKSSFFG TNSQEVGEIA GEKIMIADFQ
     KKVEEATANY TAQTGKGPSE QEQQMIREQV WNQLVLDIAY KKEFDALGLQ VSDEELVDMV
     QGNNIHPSVR QQFTNPQTGQ FDKTYVIQFL KNLKTMPAQQ QQAWANFEKS LVQDRIRSKY
     ENIMRLSNFV TSNEAQKEYQ TQTAKFNARL VHVPFYSIND STIKVENSQL EEYLAKHKEQ
     YKGYNSRSIQ YVTFPVIPTK QDTVEFYNQI KKLAKDLAVA PNDSAFAMLN SDVRTPYLVS
     YSDIPEAVKT QLGTFQVGGI YGPFKNGLTY SIYKYGGVKK DTLFTIRASH ILISPANKSD
     SAKAQAKTRA EGILAQIKGG ANFETLAQMN GMDGTAQNGG DLGYFKNNGG MVKQFEKAVF
     GFSGSGLLPS IVETDFGYHI VKVTDPKTNI SYRLAAINKN IAPSQSTLDR VYAQADNFSN
     ANGTLGAFEA ALKKDKSLIM MRADKIAENA TSINTLANAR EIVRWAFDDN TAVGDGSHKV
     FEQENQYIVA YLTAKSDKDK VKVDDYRDEI TSLVKNQLKG EKIKAKMSGL SGTLEQIAQK
     YGAGAIVENV SNISLSNGVL NTAGPDATAL GRISGMKVGK RSKAFVGDNG VYIIEKTGAT
     PAPALADYSV FKNQIQSMTS QRTSYYINEA IKENANIVDR RNKFY
//
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