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Database: UniProt
Entry: E6YZV8_BARSR
LinkDB: E6YZV8_BARSR
Original site: E6YZV8_BARSR 
ID   E6YZV8_BARSR            Unreviewed;       464 AA.
AC   E6YZV8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
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:CBI82396.1};
GN   ORFNames=B11C_40251 {ECO:0000313|EMBL:CBI82396.1}, BscR1v2_009270
GN   {ECO:0000313|EMBL:AQX30859.1};
OS   Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=687861 {ECO:0000313|EMBL:CBI82396.1};
RN   [1] {ECO:0000313|EMBL:CBI82396.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R1 {ECO:0000313|EMBL:CBI82396.1};
RX   PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA   Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA   Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT   "Parallel evolution of a type IV secretion system in radiating lineages of
RT   the host-restricted bacterial pathogen Bartonella.";
RL   PLoS Genet. 7:E1001296-E1001296(2011).
RN   [2] {ECO:0000313|Proteomes:UP000190811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1 {ECO:0000313|Proteomes:UP000190811};
RX   PubMed=28338931; DOI=10.1093/gbe/evx042;
RA   Harms A., Segers F.H., Quebatte M., Mistl C., Manfredi P., Korner J.,
RA   Chomel B.B., Kosoy M., Maruyama S., Engel P., Dehio C.;
RT   "Evolutionary Dynamics of Pathoadaptation Revealed by Three Independent
RT   Acquisitions of the VirB/D4 Type IV Secretion System in Bartonella.";
RL   Genome Biol. Evol. 9:761-776(2017).
RN   [3] {ECO:0000313|EMBL:AQX30859.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1 {ECO:0000313|EMBL:AQX30859.1};
RA   Harms A., Segers F.H.I.D., Quebatte M., Mistl C., Manfredi P., Koerner J.,
RA   Chomel B., Kosoy M., Maruyama S., Engel P., Dehio C.;
RT   "Evolutionary dynamics of pathoadaptation revealed by three independent
RT   acquisitions of the VirB/D4 type IV secretion system in Bartonella.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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; CP019789; AQX30859.1; -; Genomic_DNA.
DR   EMBL; FN645509; CBI82396.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6YZV8; -.
DR   STRING; 687861.BscR1v2_009270; -.
DR   MEROPS; S01.442; -.
DR   Proteomes; UP000190811; 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; 2.
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   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBI82396.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CBI82396.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..464
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010595935"
FT   DOMAIN          249..322
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   ACT_SITE        105
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        135
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        211
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ   SEQUENCE   464 AA;  50603 MW;  60A4630DFBAC50A0 CRC64;
     MKRSILIGLF FVIMTLISFH STNAQVPSTQ SKTTFSFAPL VKKTVPSVVN IYAARQVKVR
     SPFEDDPFFE QFFGRYQDNR PLRTQSSLGS GVIVDVRGLV VTSYHIIKGA YEIKVVLSDG
     REFESAVILK DEATDIAILE INSKDTQFPV LPLGNSDAVE VGDLVLAIGN PFGVGQTVTS
     GIVSAQARRR VGISEFDFFI QTDAAINPGN SGGALIDVNG RLIGINTAIY SRSGGSTGIG
     FAIPANLIKV VLDTVKRGEK FFVPPYIGAS FQRVTPDVAG GLGLERPYGA LVIEIVQDSP
     AAKAGLKVGD VILSVQDVQI DSPDDLIYRL ITTSVGQNLN LEYLRDGKTL KTKITVSSMS
     NSSFVKSEKI IDKSPLSGAE VLDLTPQNSQ RFHLPATVKG VVIANLDNMS NAAEIFRSGD
     ILRAVNGHQI QTVNQLKKIL MQEHPRIWQL EYERNGVYIR QFIR
//
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