ID Q2RYX4_SALRD Unreviewed; 939 AA.
AC Q2RYX4;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=X-Pro dipeptidyl-peptidase {ECO:0000313|EMBL:ABC44609.1};
GN OrderedLocusNames=SRU_2765 {ECO:0000313|EMBL:ABC44609.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44609.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC44609.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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DR EMBL; CP000159; ABC44609.1; -; Genomic_DNA.
DR RefSeq; YP_446857.1; NC_007677.1.
DR AlphaFoldDB; Q2RYX4; -.
DR STRING; 309807.SRU_2765; -.
DR ESTHER; salrd-q2ryx4; DPP4N_Peptidase_S9.
DR EnsemblBacteria; ABC44609; ABC44609; SRU_2765.
DR KEGG; sru:SRU_2765; -.
DR PATRIC; fig|309807.25.peg.2883; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_006105_3_1_10; -.
DR OrthoDB; 9812921at2; -.
DR Proteomes; UP000008674; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase 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; IPR002470; Peptidase_S9A.
DR InterPro; IPR002469; Peptidase_S9B_N.
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 PRINTS; PR00862; PROLIGOPTASE.
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:UP000008674}.
FT DOMAIN 329..627
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 718..915
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 217..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 105582 MW; 699A1EBA73677F71 CRC64;
MGSSPRSAGA ADSGRDAIHG WSPLAVAFEG GSDVACVWFS PHIPSSRLPV SSKLSSMHLS
FVRSSFVSRC SSTRVSTCPL LLVGAVLMAV VVGRPAAPAF GQEAADEEGR VGGPGAANYE
LAERFAPYKV EDMAYDLTVD LQWIEGREGF WYDFETAEGT RYWIVDPEDG TQRELFDRER
LASELTRITQ DPWDAKHLPI ENIRFVDENT LQFDVTSSQE VKDEDVEDVE EEQQKQDKEG
AGADEETEQK VFHFEYDVTT QTLRELEDYE EPDDHPDWAN VSPDGETVVF ARNYDLWMMD
GAAYEKVLDA RRGEDGEDAE EAVEELDLEE TRLTEDGEKY YSYAANNDGR GKTDTKKQEE
KGERKAVDIS WAKDSRRFAL VRSDLRDVEE LWVVHATGND RPELETFKYP MPGEDSVGRD
ELWIYDLEAM EKTRVADTGW TDQSLSILDD RQFRYPGSEA PRRRVWLSEG SDALWYERHS
RDRTKADLVV ADAETGEIER TVVEERFNKY FHTQRPELLS NGDVLWLSER DGWSHLYRYG
SDGTVEAQLT EGDWHVDAVK AVDEEEGVAY VSGNGREAGE DPYYDHLYRV QLDGSGVELL
NPGDADHSAT MNESARFFVD NHSRVDTVPR AVLRNAEGEV VTELQTADLS SLNEAGWQMP
EPFEVTAADG VTDLHGVMYK PFDFDPEKEY PVITYVYPGP QTEAVPKAFA PSGDEVGLAQ
LGFIVVVAGH RGGHPDRSRW YHTYGYGNLR DYPLADKKAT IEQLAARHDF IDGDRVGIYG
HSGGGFLTTA SLLQYPDVFD VGVASSGNHE NNVYNRWWAE THHGVEPTEN DSGEVSFDFS
IGKNSELAGN LEGDLLLTTG TIDNNVHPAN TYRMAKALIE AGKRFDLFVF PGQRHGYGSM
DDYWFWLRAE YFAEHLLSDG RDRPNVAPLQ QETPASERP
//