ID B0BW94_RICRO Unreviewed; 508 AA.
AC B0BW94;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 83.
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=degP.1 {ECO:0000313|EMBL:ABY72120.1};
GN OrderedLocusNames=RrIowa_0207 {ECO:0000313|EMBL:ABY72120.1};
OS Rickettsia rickettsii (strain Iowa).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=452659 {ECO:0000313|EMBL:ABY72120.1, ECO:0000313|Proteomes:UP000000796};
RN [1] {ECO:0000313|EMBL:ABY72120.1, ECO:0000313|Proteomes:UP000000796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa {ECO:0000313|EMBL:ABY72120.1,
RC ECO:0000313|Proteomes:UP000000796};
RX PubMed=18025092; DOI=10.1128/IAI.00952-07;
RA Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F.,
RA Hackstadt T.;
RT "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and
RT avirulent Rickettsia rickettsii Iowa.";
RL Infect. Immun. 76:542-550(2008).
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};
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP000766; ABY72120.1; -; Genomic_DNA.
DR RefSeq; WP_012150383.1; NC_010263.3.
DR AlphaFoldDB; B0BW94; -.
DR GeneID; 79936958; -.
DR KEGG; rrj:RrIowa_0207; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_5; -.
DR OMA; PIVMSAD; -.
DR Proteomes; UP000000796; 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; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABY72120.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 291..377
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 164
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 242
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 508 AA; 55606 MW; 01992F165938C8F2 CRC64;
MVNLKIVIVI IFLISSNVVL AKENSKSLKV AAQEENEFTE INSAPLKVSE AARYSFADIV
EPLIPAVVNI STIEYVNSKS ENAEKDPLQE KVNDFLEKLN IPLNLEEVDQ TPKSVPLGSG
FIIEPNGLIV TNYHVIANVD KINIKLADNT ELSAKLIGND TKTDLALLKI DSEEPLPFVE
FGDSNDARVG DWVIAIGNPF GNLGGTVTSG IISSKGRDID IDTDNIVDNF IQTDAAINNG
NSGGPMFNLD QKVIGVNTAI FSPLGTNIGI GFAIPSNTAK PIIERLKKDG KVSRGRLGVT
IQDLTEEISE GLGLKNTRGV LVAKVQEDGP GDKAGIKTGD IIIEFADIPV KNTKKLRVII
ADAPIDQEVK VKILRDKKEL ELPIKVTSDN EEVTKDSTEE TNKKEITNKE ENNLSITKNN
ITFGNLTEEL RQKYTIPQDK MGIVITNIDE EESSFKIGDL ITNINQESID DISKLEELYD
NAKKSDKQNI LLLIERGSSN MFVPLQVM
//