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Database: UniProt
Entry: A0A1A7P024_9PAST
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ID   A0A1A7P024_9PAST        Unreviewed;       346 AA.
AC   A0A1A7P024;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:OBW95190.1};
GN   ORFNames=QS62_04165 {ECO:0000313|EMBL:OBW95190.1};
OS   Gallibacterium salpingitidis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Gallibacterium.
OX   NCBI_TaxID=505341 {ECO:0000313|EMBL:OBW95190.1, ECO:0000313|Proteomes:UP000092649};
RN   [1] {ECO:0000313|EMBL:OBW95190.1, ECO:0000313|Proteomes:UP000092649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F150 {ECO:0000313|EMBL:OBW95190.1,
RC   ECO:0000313|Proteomes:UP000092649};
RA   Kudirkiene E., Bojesen A.M.;
RT   "Pan-genome of Gallibacterium spp.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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:OBW95190.1}.
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DR   EMBL; JTJL01000014; OBW95190.1; -; Genomic_DNA.
DR   RefSeq; WP_066106375.1; NZ_JTJL01000014.1.
DR   AlphaFoldDB; A0A1A7P024; -.
DR   PATRIC; fig|505341.3.peg.842; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000092649; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011783; Pept_S1C_DegS.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   NCBIfam; TIGR02038; protease_degS; 1.
DR   PANTHER; PTHR22939:SF101; PERIPLASMIC PH-DEPENDENT SERINE ENDOPROTEASE DEGQ; 1.
DR   PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092649};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          243..331
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   ACT_SITE        92
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
FT   ACT_SITE        122
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
FT   ACT_SITE        196
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611783-2"
SQ   SEQUENCE   346 AA;  37048 MW;  AD8314A30B9B25C5 CRC64;
     MIKKLLQSII IGLAAAMLIV LVLSGTSSNH FLAKFFVPQV ASYSEAVKIA APAVVNVYTR
     SLQESNSNNF DVNNLGSGVI MRSDGYILTN KHVIQNADQI IVALQSGNIY QATIIGSDWI
     TDLAVLKINA NELPTIPQNP DRQVNVGDVA LAIGNPYNLG QSVSQGIISA TGRNTISEFK
     QQNFIQTDAS INQGNSGGAL INSLGELIGI NTLSIGRSDN EVVAEGLGFA IPIKLANEVM
     NKIIKDGRVI RGFFGVESRL FSSAPIENNE QKGVLVTNLS KGGPAERAGI QIGDVIVKFG
     DITVQSPAQM VNMVAEMKPG TIVTVQVLRR NKLYNFPVEI GEYPIN
//
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