ID C5BGX1_EDWI9 Unreviewed; 684 AA.
AC C5BGX1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Protease 2, putative {ECO:0000313|EMBL:ACR69049.1};
DE EC=3.4.21.83 {ECO:0000313|EMBL:ACR69049.1};
GN OrderedLocusNames=NT01EI_1873 {ECO:0000313|EMBL:ACR69049.1};
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR69049.1, ECO:0000313|Proteomes:UP000001485};
RN [1] {ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR69049.1, ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|EMBL:ACR69049.1,
RC ECO:0000313|Proteomes:UP000001485};
RX PubMed=22247535; DOI=10.1128/JB.06522-11;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA Lawrence M.L.;
RT "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated with
RT a Natural Channel Catfish Outbreak of Enteric Septicemia of Catfish.";
RL J. Bacteriol. 194:740-741(2012).
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DR EMBL; CP001600; ACR69049.1; -; Genomic_DNA.
DR RefSeq; WP_015871195.1; NC_012779.2.
DR AlphaFoldDB; C5BGX1; -.
DR STRING; 67780.B6E78_02410; -.
DR MEROPS; S09.010; -.
DR GeneID; 69538820; -.
DR KEGG; eic:NT01EI_1873; -.
DR PATRIC; fig|634503.3.peg.1679; -.
DR HOGENOM; CLU_011290_0_1_6; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000001485; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ACR69049.1};
KW Protease {ECO:0000313|EMBL:ACR69049.1}.
FT DOMAIN 7..408
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 466..679
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 684 AA; 78691 MW; 2FC6437A8FACEA3A CRC64;
MKKAPKAAKH PYEIVMHGDR RVDDYYWLRD DTRSDPQVLA YLNAENAYSE RCLAPQSALR
SALLAEMVAR IPQQDASVPY VRNGYRYQHR YRPAAEYAEY WRQPESACPE NETAWQRLLD
TNQRAEGHDF YALGALEVSP DNRLLAISED TVSRRQYTLR VKSLMDDIWL EESIEGCDGH
IEWCNDSRAF YYIRLDPQTL LPYQIYRHRL GTPCSQDCLI YQELDDAFYL GLEKSLSQRY
VMIHISSTTT SEVLLLDADD PEARAHCFQP RRRDHEYSLE HYDSRFYIRS NREGQNFALY
CGPDGDVLSW QTLVPPRDAV MLEDFCLFQE WLVVEERTHG LTTLRQIRRD DGEERLIHFD
DPTYVTWLGY NPQPEIAKLR YGYASMTTPG SVYELDLNSG ERRLLKQQSV AEFSAQDYAS
ERIWLRARDG VDVPVSLVYR RDRFVRGQNP ILIYGYGAYG SSMDPGFSTS RLSLLDRGFV
FALAHVRGGA DLGQQWYEDG KLLHKLNSFY DFIDVTQGLV RQGYAATDQV YAMGGSAGGL
LVGGVLNMAP QLYRGAVAQV PFVDVVTTML DPSIPLTTGE YDEWGNPEDP EYYHYMQRYS
PYDGVRAQAY PHLLVTTGLH DSQVQYWEPA KWVARLREMK CDDNLLLLHT DMEAGHGGKS
GRFKAYEDIA LEYAFILTLS GVTQ
//
