ID A0A223P1U6_9SPHI Unreviewed; 702 AA.
AC A0A223P1U6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=MuYL_4244 {ECO:0000313|EMBL:ASU36129.1};
OS Mucilaginibacter xinganensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1234841 {ECO:0000313|EMBL:ASU36129.1, ECO:0000313|Proteomes:UP000215002};
RN [1] {ECO:0000313|EMBL:ASU36129.1, ECO:0000313|Proteomes:UP000215002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJC16-A31 {ECO:0000313|EMBL:ASU36129.1,
RC ECO:0000313|Proteomes:UP000215002};
RG Henan University of Science and Technology;
RA You X.;
RT "Complete genome sequence of Mucilaginibacter sp. strain BJC16-A31.";
RL Submitted (AUG-2017) 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}.
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DR EMBL; CP022743; ASU36129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223P1U6; -.
DR KEGG; muc:MuYL_4244; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000215002; Chromosome.
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; -; 2.
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; PF13145; Rotamase_2; 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; 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:ASU36129.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000215002};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 347..444
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 702 AA; 76794 MW; 3BB5C8E9709B61D4 CRC64;
MGIMGFLRER MGKILAFFIG LALLAFIVGE VVRSGGSFFR DDRNLLGEVG GEKVAYDEYN
KRYEQNTAQF KQQSGQANLT PQIVAYVQEN TWNTVISQMI LNKEVDKLGL VVGDDETKSM
ISGNNPDQQI VQAFGNPQTG KVDMNKLNTF LTNLNASKAD DPLRQQWRDF TTQLIESKLS
QKYVAIVTNG LYVNSLDAKD DYTAKNKLAN FKYVSLDYAS VPDNKITVTD ADYQSYYDEH
KTEFKAAQEL RTFNYVSFNA SPSKADSAAI KQQAEKVATE FKASSNDSLF VQINSETKMP
LVYLHKGRLE PKLDSVMFNA SKGFMYGPYL SGSSYKIAKL VDTRVEPDSV KARHILIDDK
SIGLDKAMAK ADSLKKLIEG GKSFADLANL YSVDKNSAVK GGDLGTFGRG AMIPVFDDAV
FEAKKGDLKI VASQFGVHLF QVEDQKGSSK VVKVALVDVP LKSSSATQTA AYSKAQAFLG
TLTKENFDAT AKKEGLQLKT ASDVTGIAAS FPGVESGRDI VKWAFGAEKG DFSDKVYITG
DQYIVAHLTE VKPKGQLSLD AVKKQIESLV KNKVKGKQLV DKLQGALNGS STIDQVAQKA
GSKVVPLQNI VFANPVIPGS SAEYKVIGTV FGSQPNKLSK PVEGQQGVFV FSVDSFINPA
ALTNAVREKD QLGQALLQRA EPQLFDALKD KANVKDYRAK FL
//
