ID B0VTL9_ACIBS Unreviewed; 476 AA.
AC B0VTL9;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
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};
GN OrderedLocusNames=ABSDF0946 {ECO:0000313|EMBL:CAP00306.1};
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP00306.1, ECO:0000313|Proteomes:UP000001741};
RN [1] {ECO:0000313|EMBL:CAP00306.1, ECO:0000313|Proteomes:UP000001741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF {ECO:0000313|EMBL:CAP00306.1,
RC ECO:0000313|Proteomes:UP000001741};
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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}.
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DR EMBL; CU468230; CAP00306.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VTL9; -.
DR KEGG; abm:ABSDF0946; -.
DR HOGENOM; CLU_020120_1_0_6; -.
DR BioCyc; ABAU509170:GCL9-759-MONOMER; -.
DR Proteomes; UP000001741; Chromosome.
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; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CAP00306.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 261..332
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 383..452
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 476 AA; 51306 MW; E85E7F8EA83C6A33 CRC64;
MIQKFYSYSR RPIVGEHRMK SRYLQQGMYA AVFTVAAVQA NAAVDFSNLV EQVSPAVVSV
NVVKKMTQDE LLQQQVPEIL KRFFGNQVII PQQQGPQEKT AYGSAFFISK DGYLLTNHHV
IENASRISIT LNDRREIDAT VVGSDERTDV ALLKVNGTNY PALRVGNVDR LRVGESVLAI
GSPFGFDYSA SAGIVSAKSR NMSGETSVPF IQTDVALNPG NSGGPLFNQN GEVVGVNSRI
FSGTGGYMGL SFSIPIDVAM DVAEQLKTKG KVTRSYLGVM MQDIDRNLAD AYKLPKPEGA
LITQVSPNSP AQKAGLRAGD VILKLNGASV LRTSDLLYAL NKVQPNQTVQ FEVLRDDKTR
NISATLATAP DETPATGNQA SASKGPVLGM SIRDLAVPEK NALGIKGGIY VQDVRRGGLA
SLSNIIPGDV IIQVNNTQIL NSQDFAKVVS NLPKNTVARV GIIRQGQRAM LGLRIQ
//