ID   Q44476_AZOVI            Unreviewed;       473 AA.
AC   Q44476;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE            EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
DE   AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
OS   Azotobacter vinelandii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354 {ECO:0000313|EMBL:AAB01513.1};
RN   [1] {ECO:0000313|EMBL:AAB01513.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UW 136 {ECO:0000313|EMBL:AAB01513.1};
RX   PubMed=8606151;
RA   Martinez-Salazar J.M., Moreno S., Najera R., Boucher J.C., Espin G.,
RA   Soberon-Chavez G., Deretic V.;
RT   "Characterization of the genes coding for the putative sigma factor AlgU
RT   and its regulators MucA, MucB, MucC, and MucD in Azotobacter vinelandii and
RT   evaluation of their roles in alginate biosynthesis.";
RL   J. Bacteriol. 178:1800-1808(1996).
CC   -!- FUNCTION: Might be efficient in the degradation of transiently
CC       denatured and unfolded proteins which accumulate in the periplasm
CC       following stress conditions. {ECO:0000256|ARBA:ARBA00002610}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Acts on substrates that are at least partially unfolded. The
CC         cleavage site P1 residue is normally between a pair of hydrophobic
CC         residues, such as Val-|-Val.; EC=3.4.21.107;
CC         Evidence={ECO:0000256|ARBA:ARBA00001772};
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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DR   EMBL; U30799; AAB01513.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q44476; -.
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; 2.
DR   Gene3D; 2.30.42.10; -; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR22939:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR   PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   Pfam; PF13180; PDZ_2; 2.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..473
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004231822"
FT   DOMAIN          266..339
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          374..462
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          150..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  50282 MW;  C97B357D897738AB CRC64;
     MSKVGFKSFA SVLAGALLLG QSLFVQAQLP EFTSLVEEAS PAVVNISTRQ KLPDRSTVQG
     LPDLEGLPPL FREFLERSIP QLPRTPDNGR QREAHSLGSG FIISPDGYVL TNNHVVADAD
     EIIVRLSDRS ELEAELVGAD PLTRCSFVEG QGFESPHSQT GTYRPIESRG MGSGHRFPFR
     FRSFRDCGHH QCHGAKPAER ELVPFIQTDV AINPGNSGGP LFDLDGRVIG INSQIFTRSG
     GFMGLSFAIP IEVAMGVADQ LKATGKVARG WLGVIIQEVN KDLAESFGLD RPAGALVAQV
     LEDGPADKGG LQVGDVILSL DGHPIVMSAD LPHLVGGLKP GAAANLEVVR DGKRRNIAIT
     VGALPEEGNG VQPSIAGTEQ SSNRLGVTVT ELTAEQKKSL DLKGGVVIRE VLNGPAALIG
     LRPGDVVTHL NNQPIDSAKT FAEVAGALPK GRSVSMRVLR QGRASFITFK LAE
//