ID F0REK7_CELLC Unreviewed; 841 AA.
AC F0REK7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Peptidase S9B dipeptidylpeptidase IV domain protein {ECO:0000313|EMBL:ADY31022.1};
GN OrderedLocusNames=Celly_3205 {ECO:0000313|EMBL:ADY31022.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY31022.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY31022.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
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DR EMBL; CP002534; ADY31022.1; -; Genomic_DNA.
DR RefSeq; WP_013622765.1; NC_015167.1.
DR AlphaFoldDB; F0REK7; -.
DR STRING; 867900.Celly_3205; -.
DR ESTHER; cellc-f0rek7; DPP4N_Peptidase_S9.
DR KEGG; cly:Celly_3205; -.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_006105_3_1_10; -.
DR OrthoDB; 9812921at2; -.
DR Proteomes; UP000007487; 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; 1.
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:UP000007487};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..841
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003259295"
FT DOMAIN 172..531
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 616..806
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 138..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 96454 MW; B2E749D7E229A0E8 CRC64;
MIKKMALLLL FAVCTTVTFA QEETSNVPTP NYRQAAKFSP DNLKKIVHST TVRPNWLKKG
NRFWYQYKTT EGANFYLVDA DRGTKTKLFD NAKMAQWLTL ITKDPYDAKH LPRFNFKFVK
NETAIRFRVT SKEKVDVVDD KKDDKKNDTI SKDSTKAKSA KKAPKKENKV YYLEYKLGGN
GLTVINNKKE DENKKRWANI APDSSIVLFS KQHNLYWMDK ANYLKAVKDE KDSTIVEHQW
TKDGVENYGY GGGSWGENNE TKEENKDKRK GIRGYWSHDS KKFVYQRSDS RDLKDLWVIN
SVAKKRPTLE TYKYHMPGEK EFSKPEILVF DIPSKEKRAV KLDTTIQQSI DIYSAPTKKM
NFSDDFRPSL LLSKKGKIYF SSTSRDRKKV HINVADINTG EVKTLIKEEL NTYVEAKDIV
LFNNEQEIIQ WSERDGWAHF YLYDANGNLK NQITKGSYHS NSFVGVNEKE RTLFFTANGV
TKEQDPYYEH LFKINLNGTG LKNLNKGDYN TSTSMADSNR FFVNNYSRVN TVPKSELRSS
NGNVVLKLEE ADLSALMSTG YKFPEPFKVK ADDGITDLYG VMYKPFDFDE TKSYPLIEYV
YPGPQTEAVN KSFSVSMNRL DRLAQVGFVV VTLGNRGGHP NRSKWYHNYG YGNLRDYGLA
DKKYVAEQLA DKHNFIDISK VGIFGHSGGG FMSTAAMLVY PDFFKVAVSS AGNHDNSMYN
SWWSETHHGV EEVKDANGVI TYKYDIDKNQ TLAANLKGKL MLVTGDVDNN VHPGATIRMA
NALIKANKRF DFMIMPGQRH GFGSMTEYFF WLKADYFSKH FLGVEATNVD MLEMNRAKPK
H
//