ID   DEGPL_BARHE             Reviewed;         503 AA.
AC   P54925; Q6G491;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Probable periplasmic serine endoprotease DegP-like;
DE            EC=3.4.21.107;
DE   AltName: Full=Antigen HtrA;
DE   AltName: Full=Protease Do;
DE   Flags: Precursor;
GN   Name=htrA; OrderedLocusNames=BH04770;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=8027347; DOI=10.1128/jcm.32.4.942-948.1994;
RA   Anderson B., Sims K., Regnery R., Robinson L., Schmidt M.J., Goral S.,
RA   Hager C., Edwards K.;
RT   "Detection of Rochalimaea henselae DNA in specimens from cat scratch
RT   disease patients by PCR.";
RL   J. Clin. Microbiol. 32:942-948(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC   -!- FUNCTION: Could 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; L20127; AAA97430.1; -; Genomic_DNA.
DR   EMBL; BX897699; CAF27285.1; -; Genomic_DNA.
DR   RefSeq; WP_011180408.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; P54925; -.
DR   SMR; P54925; -.
DR   STRING; 283166.BH04770; -.
DR   PaxDb; P54925; -.
DR   PRIDE; P54925; -.
DR   EnsemblBacteria; CAF27285; CAF27285; BH04770.
DR   GeneID; 64156758; -.
DR   KEGG; bhe:BH04770; -.
DR   eggNOG; COG0265; Bacteria.
DR   OMA; RALFQIQ; -.
DR   Proteomes; UP000000421; Chromosome.
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; IPR041489; PDZ_6.
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; 1.
DR   Pfam; PF17820; PDZ_6; 1.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..503
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_0000026923"
FT   DOMAIN          286..357
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          419..466
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        143
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        173
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        247
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   BINDING         245..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         302..306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        285..286
FT                   /note="KQ -> NE (in Ref. 1; AAA97430)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        430
FT                   /note="V -> L (in Ref. 1; AAA97430)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  54113 MW;  B257E7B9FD9835D8 CRC64;
     MVKKTFFTTL AAVSFSAALE TALFFSGCGS SLWTTKAHAN SVFSSLMQQQ GFADIVSQVK
     PAVVSVQVKS NKKKKEWFFS DFFSTPGFDQ LPDQHPLKKF FQDFYNRDKP SNKSLQRSHR
     LRPIAFGSGF FISSDGYIVT NNHVISDGTS YAVVLDDGTE LNAKLIGTDP RTDLAVLKVN
     EKRKFSYVDF GDDSKLRVGD WVVAIGNPFG LGGTVTAGIV SARGRDIGTG VYDDFIQIDA
     AVNRGNSGGP TFDLNGKVVG VNTAIFSPSG GNVGIAFAIP AATAKQVVQQ LIEKGLVQRG
     WLGVQIQPVT KEISDSIGLK EAKGALITDP LKGPAAKAGI KAGDVIISVN GEKINDVRDL
     AKRIANMSPG ETVTLGVWKS GKEENIKVKL DSMPEDENMK DGSKYSNEHG NSDETLEDYG
     LIVAPSDDGV GLVVTDVDPD SDAADKGIRP GDVIVTVNNK SVKKVSDITD TIKNAQKLGR
     KAILLQVRTN DQNRFVALPI FKK