ID E4TSQ2_MARTH Unreviewed; 791 AA.
AC E4TSQ2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Peptidase S9B dipeptidylpeptidase IV domain protein {ECO:0000313|EMBL:ADR21862.1};
GN OrderedLocusNames=Ftrac_1875 {ECO:0000313|EMBL:ADR21862.1};
OS Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408
OS / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter tractuosus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Marivirgaceae; Marivirga.
OX NCBI_TaxID=643867 {ECO:0000313|EMBL:ADR21862.1, ECO:0000313|Proteomes:UP000008720};
RN [1] {ECO:0000313|EMBL:ADR21862.1, ECO:0000313|Proteomes:UP000008720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 /
RC H-43 {ECO:0000313|Proteomes:UP000008720};
RX PubMed=21677852; DOI=10.4056/sigs.1623941;
RA Pagani I., Chertkov O., Lapidus A., Lucas S., Del Rio T.G., Tice H.,
RA Copeland A., Cheng J.F., Nolan M., Saunders E., Pitluck S., Held B.,
RA Goodwin L., Liolios K., Ovchinikova G., Ivanova N., Mavromatis K., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Han C., Tapia R., Ngatchou-Djao O.D., Rohde M., Goker M., Spring S.,
RA Sikorski J., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Marivirga tractuosa type strain (H-43).";
RL Stand. Genomic Sci. 4:154-162(2011).
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DR EMBL; CP002349; ADR21862.1; -; Genomic_DNA.
DR RefSeq; WP_013454005.1; NC_014759.1.
DR AlphaFoldDB; E4TSQ2; -.
DR STRING; 643867.Ftrac_1875; -.
DR ESTHER; marth-e4tsq2; DPP4N_Peptidase_S9.
DR KEGG; mtt:Ftrac_1875; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_019735_0_0_10; -.
DR OrthoDB; 9812921at2; -.
DR Proteomes; UP000008720; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF193; DIPEPTIDYL PEPTIDASE 9; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008720};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..791
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003187293"
FT DOMAIN 236..504
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 594..790
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 791 AA; 90724 MW; 56EA9DE4C9C5C744 CRC64;
MKKLVLSLLL VILYGSTSIA QEIGELSVQK IMRDPAWIGH SPDNFYWGEN NDQLFFNWNP
QDHPDDSLYA YNFEKGEAIL ISHEEELKYP DRRGIYNKAR TEKLFIRDGN LYLSEIKTGN
IEPLIESSQR ISNTGFLLDE QKIFYVVNNN IFTWDRKSGK TRQLVEFSKE AEPKEKSAKK
SDKEEWLNNQ QLELFSVLKE NKERKEKSDE YKESIKSDGI PTIYLDGKRL IESIISPDGN
YVIYRLYISP KGDDNTIVPD YVTESGYTKD LNARSKVGGE QAHMELGVFN LKTRESKIVN
IDEVEGLKQI PEFWSDYPER KEEDFESRKM IFQSPLFSDD GNFVVIDARA TDNKDRWLFL
LNPETAKLDL VDRQRDEAWI AGPGVGYAWG GSTKGFLADN KTLYFQSEES GYSHLYSVDL
SKTKKKKKQL TKGEFEIYDV NLSNDKNHFY FLANPESPGI RNLYKLPVSG GKMEQLTSDK
GGMEYALAPD ESKIAIRKST AAQPWELYVM DNQPNAEAKR ITNSISDEFK SYDWRTPEYI
TFEAEDGAEV HARLYQPEGG SNGKPAVIFV HGAGYLQNAH QWWSSYFREY MFHNLLADNG
YTVLDIDYRG SAGYGRDWRT GIYRHMGGKD LSDQVDGAKY LVDELGVDEE NIGIYGGSYG
GFITLMALFN EAETFKSGAA LRSVTDWAHY NHGYTSNILN TPVDDPIAYE RSSPIYFAEG
LEGNLLIAHG MVDTNVHFQD VVRLSQRLIE LGKENWEMAV YPVESHGFVE PSSWTDEYRR
IFELFEDTLK E
//