ID A0A2T7Q717_9BACT Unreviewed; 705 AA.
AC A0A2T7Q717;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=DC498_17065 {ECO:0000313|EMBL:PVD51124.1};
OS Terrimonas sp.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Terrimonas.
OX NCBI_TaxID=1914338 {ECO:0000313|EMBL:PVD51124.1, ECO:0000313|Proteomes:UP000244333};
RN [1] {ECO:0000313|EMBL:PVD51124.1, ECO:0000313|Proteomes:UP000244333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS-102 {ECO:0000313|EMBL:PVD51124.1,
RC ECO:0000313|Proteomes:UP000244333};
RA Zhang L., Jiang J.;
RT "The draft genome of strain NS-102.";
RL Submitted (APR-2018) 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:PVD51124.1}.
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DR EMBL; QCZJ01000016; PVD51124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7Q717; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000244333; 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; 1.10.8.1040; -; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000244333};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 344..448
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 705 AA; 77659 MW; F131F8D8BD2B9CE7 CRC64;
MSIIETLRKR AGILVIAIAV SLIGFIVQDA FFGRGGGVKE PSKTIGKING TNIDRQDFDA
RVKMMEAQYQ SQGYRIEEGM RQEIQNQVWN SLVSRELILS EAKKLGIDFT SKEFSELLFS
DNAPQEFKQQ FTDPKTGVYN IEAARNAFLT LKKSKNAEQI KQVNEQLIDP IVLNQVQQKF
FTIFTNGAYI PKWLIEKQNA VNGQVSDIAY TGLSYSSIAD SAAVVSDADI NDYIQKHKDQ
FKQEKSRSIA FVTFNAGANK EDSANLWNKM EGMKQALTDA PDAGVFVTRN GTKSPFFDGY
INKSRIQVPS KDSLLALQPG QVYGPYYDAN TIVVARMIGS KVLPDSVKAR HILIGTIDLQ
TQQPSRTDSA AKALADSIKN AIAGGASFVE LAAKYSDDLG SKDQGGEYNY FPNGQMVKEF
NDFCFEGKTG DKGVIKTQFG YHYIEVQDQK NFETAYKIAY LAKTIEPSKE TDDAASAAAT
KFASESRTEK AFDDAVAKNK FNKRIADNIK EMDYQVAGLT PSRSFVKWVY ENKPGTVSDP
ISVGDQYVVA AITGEKPAGV QSAATAKLAI EPILRNKKKA AMLVQKFGKY SSIDEAAKNT
DQQVQTTDSI RFSDNFKPGF GNELIVIGAS FDKAYQGKPS QPLTGTTGVY VVEVKNIGAL
PNDAANVEEQ RKAALMQMRQ TMGYGLMEAL KEAANIQDTR LKAGY
//
