ID Q1RHB3_RICBR Unreviewed; 512 AA.
AC Q1RHB3;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
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 Name=htrA {ECO:0000313|EMBL:ABE05251.1};
GN OrderedLocusNames=RBE_1170 {ECO:0000313|EMBL:ABE05251.1};
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407 {ECO:0000313|EMBL:ABE05251.1, ECO:0000313|Proteomes:UP000001951};
RN [1] {ECO:0000313|EMBL:ABE05251.1, ECO:0000313|Proteomes:UP000001951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C {ECO:0000313|EMBL:ABE05251.1,
RC ECO:0000313|Proteomes:UP000001951};
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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}.
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 Evidence={ECO:0000256|ARBA:ARBA00001772};
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DR EMBL; CP000087; ABE05251.1; -; Genomic_DNA.
DR RefSeq; WP_011477829.1; NC_007940.1.
DR AlphaFoldDB; Q1RHB3; -.
DR KEGG; rbe:RBE_1170; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_5; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000001951; 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; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.42.60; -; 1.
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; 1.
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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABE05251.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ABE05251.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001951};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 296..382
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 247
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 512 AA; 55971 MW; A8741EBD7B823C3D CRC64;
MNLKIFFIII ILIFNNNILA KENNKSSKAI DLEEESEFTE INSIPLKVNN ASRYSFADIV
EPLIPAVVNI STIEYVNSKS EAAEKDPLQE KKPLDFINDF LERLNIPLNL EEVDPTPKAM
PLGSGFIIEP NGLIVTNYHV IANVSKINVK LADNTELPAK LIGSDTKTDL ALLKIDVEEP
LPFVEFGDSN DARVGDWVIA IGNPFGNLGG TVTAGIISSK GRDIDIDTNN IVDNFIQTDA
AINNGNSGGP MFNLDQKVIG VNTAIFSPLG TNIGIGFAIP SNTAKPIIER LKKDGKINRG
RLGVTIQDLT EEISEGLGLK DTNGVLVAKI QKDDPGDKAG IKTGDIILEF AGQTVKNTKR
LRVIVADIPV DQEVKVKVLR DGEAIELPIK MTSDNEEVKQ EAAEENIEKV TKKEDNGTSI
TKSNITFSNL TEELKQKFAI SVDKVGLVIT NVDEEDSSFR VGDLVSNVNQ ESISDINKLE
ELYENAKKSE KQNILLLIER GDSSMFVPLS VM
//
