DEGPL_BRUME
ID DEGPL_BRUME Reviewed; 513 AA.
AC Q8YG32;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=BMEI1330;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008917; AAL52511.1; -; Genomic_DNA.
DR PIR; AD3418; AD3418.
DR RefSeq; WP_004683321.1; NZ_GG703778.1.
DR AlphaFoldDB; Q8YG32; -.
DR SMR; Q8YG32; -.
DR STRING; 224914.BMEI1330; -.
DR EnsemblBacteria; AAL52511; AAL52511; BMEI1330.
DR GeneID; 29594176; -.
DR KEGG; bme:BMEI1330; -.
DR PATRIC; fig|224914.52.peg.76; -.
DR eggNOG; COG0265; Bacteria.
DR OMA; RALFQIQ; -.
DR PhylomeDB; Q8YG32; -.
DR PRO; PR:Q8YG32; -.
DR Proteomes; UP000000419; 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_0000026924"
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; 53514 MW; C472FEF99DFC6268 CRC64;
MSRARISNYR KGVAAVALSA ALAGAFVVTG PLGALNEARA EAVHVTPPQQ 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