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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//