DEGPL_BRUSU
ID DEGPL_BRUSU Reviewed; 513 AA.
AC P0A3Z5; G0K7M9; Q44597;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable periplasmic serine endoprotease DegP-like;
DE EC=3.4.21.107;
DE AltName: Full=Protease Do;
DE Flags: Precursor;
GN Name=htrA; OrderedLocusNames=BR0611, BS1330_I0607;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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:0000250}.
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AE014291; AAN29540.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM17957.1; -; Genomic_DNA.
DR RefSeq; WP_002963760.1; NZ_KN046804.1.
DR AlphaFoldDB; P0A3Z5; -.
DR SMR; P0A3Z5; -.
DR EnsemblBacteria; AEM17957; AEM17957; BS1330_I0607.
DR GeneID; 45124069; -.
DR GeneID; 55590344; -.
DR KEGG; bms:BR0611; -.
DR KEGG; bsi:BS1330_I0607; -.
DR PATRIC; fig|204722.22.peg.1292; -.
DR HOGENOM; CLU_020120_1_0_5; -.
DR OMA; RALFQIQ; -.
DR PhylomeDB; P0A3Z5; -.
DR PRO; PR:P0A3Z5; -.
DR Proteomes; UP000007104; Chromosome I.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 2.
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 Pfam; PF13180; PDZ_2; 2.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR TIGRFAMs; TIGR02037; degP_htrA_DO; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 3: Inferred from homology;
KW Hydrolase; Periplasm; Protease; Repeat; Serine protease; Signal;
KW Stress response.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..513
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /id="PRO_0000026926"
FT DOMAIN 300..391
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 414..500
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 100..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..299
FT /note="Serine protease"
FT REGION 403..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 257
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT BINDING 255..257
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 312..316
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 513 AA; 53483 MW; DE1CEF1959472806 CRC64;
MSRARISNYR KGVAAVALSA ALAGAFVVTG PLGALNEARA EAVHVTPPPQ AGFADLVEKV
RPAVVSVRVK KDVQETSNRG PQFFGPPGFD QLPDGHPLKR FFRDFGMEPR GDSRSDNRRG
KANKPRPGHE RPVAQGSGFV ISEDGYVVTN NHVVSDGDAY TVVLDDGTEL DAKLIGADPR
TDLAVLKINA PKRKFVYVAF GDDNKVRVGD WVVAVGNPFG LGGTVTSGIV SARGRDIGAG
PYDDFIQIDA AVNKGNSGGP AFDLSGEVIG INTAIFSPSG GSVGIAFAIP SSTAKQVVDQ
LIKKGSVERG WIGVQIQPVT KDIAASLGLA EEKGAIVASP QDDGPAAKAG IKAGDVITAV
NGETVQDPRD LARKVANIAP GEKAALTVWR KNKAEEINVT IAAMPNDKGK SGSQSNDNDG
GQGETLDSYG LTVVPSEDGK GVVVTDVDPD SDAADRGIRS GDVIVSVNNQ TVKTAGDINK
AITAAEKSGR KAVLLQLQSN DQSRFVALPI NQE
