ID   DEGPL_BRUA2             Reviewed;         513 AA.
AC   Q2YMX6; P0A3Z6; Q44597; Q57EC9;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=BAB1_0635;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=7861951; DOI=10.1006/mpat.1994.1049;
RA   Tatum F.M., Cheville N.F., Morfitt D.;
RT   "Cloning, characterization and construction of htrA and htrA-like mutants
RT   of Brucella abortus and their survival in BALB/c mice.";
RL   Microb. Pathog. 17:23-36(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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; U07352; AAA70164.1; -; Genomic_DNA.
DR   EMBL; AM040264; CAJ10591.1; -; Genomic_DNA.
DR   PIR; I40060; I40060.
DR   RefSeq; WP_002963760.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YMX6; -.
DR   SMR; Q2YMX6; -.
DR   STRING; 359391.BAB1_0635; -.
DR   PRIDE; Q2YMX6; -.
DR   EnsemblBacteria; CAJ10591; CAJ10591; BAB1_0635.
DR   GeneID; 45124069; -.
DR   GeneID; 55590344; -.
DR   KEGG; bmf:BAB1_0635; -.
DR   PATRIC; fig|359391.11.peg.2948; -.
DR   HOGENOM; CLU_020120_1_0_5; -.
DR   OMA; RALFQIQ; -.
DR   PhylomeDB; Q2YMX6; -.
DR   Proteomes; UP000002719; 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; Reference proteome; Repeat;
KW   Serine protease; Signal; 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_0000093858"
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