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Database: UniProt
Entry: C7NDM4_LEPBD
LinkDB: C7NDM4_LEPBD
Original site: C7NDM4_LEPBD 
ID   C7NDM4_LEPBD            Unreviewed;       298 AA.
AC   C7NDM4;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=PpiC domain-containing protein {ECO:0000259|PROSITE:PS50198};
GN   OrderedLocusNames=Lebu_0266 {ECO:0000313|EMBL:ACV38186.1};
OS   Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS   10249 / C-1013-b).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV38186.1, ECO:0000313|Proteomes:UP000001910};
RN   [1] {ECO:0000313|EMBL:ACV38186.1, ECO:0000313|Proteomes:UP000001910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b
RC   {ECO:0000313|Proteomes:UP000001910};
RX   PubMed=21304648; DOI=10.4056/sigs.1854;
RA   Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA   Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA   Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT   b).";
RL   Stand. Genomic Sci. 1:126-132(2009).
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DR   EMBL; CP001685; ACV38186.1; -; Genomic_DNA.
DR   RefSeq; WP_012806373.1; NC_013192.1.
DR   AlphaFoldDB; C7NDM4; -.
DR   STRING; 523794.Lebu_0266; -.
DR   KEGG; lba:Lebu_0266; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_933171_0_0_0; -.
DR   OrthoDB; 82234at2; -.
DR   Proteomes; UP000001910; Chromosome.
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; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   PANTHER; PTHR47245:SF2; SLR0208 PROTEIN; 1.
DR   Pfam; PF13145; Rotamase_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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..298
FT                   /note="PpiC domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007912113"
FT   DOMAIN          148..245
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   298 AA;  33235 MW;  5C70637D6F3A1A10 CRC64;
     MKNKIKIGVL TVLCVFALSC KNNAGQSGKV LFESPDKQIK VYENEVNNEL AKSLYSSGVD
     EKDLTSDQIA QMKQSIIKNI ALNRALAIKG KEKKLDQDKK YTESTDILQE QLLASLATLN
     EVNDKAKVTD ADAKNIYDAN AANFTRQEDS VRLQLIVFNT SDSAKANQVL KEAIANPADF
     TSYARKYNAN IQGVTENGET QEIPLTQLSS RFGPLNEAIK DVKAGQIVNK VVTVGNDLYV
     VKVLERNGKG LIPFEKVKET IKTQLRNQKR QVEQQKYLKS ISDEFKLSNM DEALKNIK
//
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