ID W1S7K2_9SPHN Unreviewed; 754 AA.
AC W1S7K2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Peptidase S9 {ECO:0000313|EMBL:ETI63999.1};
GN ORFNames=C100_09635 {ECO:0000313|EMBL:ETI63999.1};
OS Sphingobium sp. C100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1207055 {ECO:0000313|EMBL:ETI63999.1, ECO:0000313|Proteomes:UP000018867};
RN [1] {ECO:0000313|EMBL:ETI63999.1, ECO:0000313|Proteomes:UP000018867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C100 {ECO:0000313|EMBL:ETI63999.1,
RC ECO:0000313|Proteomes:UP000018867};
RX PubMed=24482512;
RA Dong C., Bai X., Lai Q., Xie Y., Chen X., Shao Z.;
RT "Draft Genome Sequence of Sphingobium sp. Strain C100, a Polycyclic
RT Aromatic Hydrocarbon-Degrading Bacterium from the Deep-Sea Sediment of the
RT Arctic Ocean.";
RL Genome Announc. 2:0-0(2014).
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:ETI63999.1}.
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DR EMBL; AYOY01000138; ETI63999.1; -; Genomic_DNA.
DR RefSeq; WP_024019580.1; NZ_AYOY01000138.1.
DR AlphaFoldDB; W1S7K2; -.
DR STRING; 1207055.C100_09635; -.
DR PATRIC; fig|1207055.3.peg.1804; -.
DR eggNOG; COG1506; Bacteria.
DR OrthoDB; 1094230at2; -.
DR Proteomes; UP000018867; Unassembled WGS sequence.
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:UP000018867};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..754
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004809043"
FT DOMAIN 174..463
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 553..749
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 102..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 82338 MW; 8726DA6E6998EDE2 CRC64;
MPPYLKCGAA FCALLLIPAL PAQAFAQAQA PTQAPTQAAK KLTLERVFAS PDLAGPQPRA
LKLSPDGALV TLLKPRPDEK ERLDLWAIDT RTGAERMLVD SKKTGSGAEL SEAEKMQRER
DRSVAGSTGI TGYDWSPDGK SILVPVDGDL YLAALDGQVT RLTDTPEGEL NGVVSPGGSF
VSFVRDGNLF VQPIDGAERQ VTKGASDTVS WGVAEFVAQE EMDRRTGYWW SPDDSLIAVA
RVDESPVGIV TRTAIGGEGT KVYQQRYPAA GTPNAIVELY VMKPDGSSQV KVDLGADKDV
YLARVDWSKD GKTLYVQRES RDQKRLDLLA VDPATGAAKV ALTETAKSWI NLSNSFHPLR
DGSFLWWSER TGHGHLYRVH ESKWTALTSG DWEVRDVVGV DETKGLVYFT GNRETPLEQQ
LYVTTLGKLA PARALTQAGW WNDAVMDRAA TRIVVTRQNS DQPKQLYLAD SSGKQLQWLS
ENALTGDHPY APYVASHAKT RFGTVKAADG TTLYTKIMTP PMEPGKRYPV FMIHYGGPGG
GRQVTNSWSG ALNQYLVDRG WIVFAIDNRG TPDRGKAFED HLYRAMGTVE VEDQLKGVEW
LKAQPYVDPN RIATYGWSYG GYMSVKLLEK ATGVFAAAVA GAPVTKWQLY DTHYTERYLG
QPQDKPSAYP AAGAVDDAVK ITDPLLLIHG MSDDNVVFDN ATALMAKMQG AAVPFEMMAY
PGQTHRVGGP GISVHVWRTI EHFLAEHAGG PAED
//
