ID E7G583_9HELI Unreviewed; 475 AA.
AC E7G583;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Protease DO {ECO:0000313|EMBL:EFX41448.1};
GN Name=degP {ECO:0000313|EMBL:EFX41448.1};
GN ORFNames=HSUHS5_1166 {ECO:0000313|EMBL:EFX41448.1};
OS Helicobacter suis HS5.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=710394 {ECO:0000313|EMBL:EFX41448.1, ECO:0000313|Proteomes:UP000054093};
RN [1] {ECO:0000313|EMBL:EFX41448.1, ECO:0000313|Proteomes:UP000054093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS5 {ECO:0000313|EMBL:EFX41448.1,
RC ECO:0000313|Proteomes:UP000054093};
RX PubMed=21414191; DOI=10.1186/1297-9716-42-51;
RA Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A.,
RA De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.;
RT "Genome sequence of Helicobacter suis supports its role in gastric
RT pathology.";
RL Vet. Res. 42:51-51(2011).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFX41448.1}.
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; ADHO01000259; EFX41448.1; -; Genomic_DNA.
DR AlphaFoldDB; E7G583; -.
DR MEROPS; S01.500; -.
DR Proteomes; UP000054093; Unassembled WGS sequence.
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; -; 2.
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; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 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:0000313|EMBL:EFX41448.1};
KW Protease {ECO:0000313|EMBL:EFX41448.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054093};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..475
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039425914"
FT DOMAIN 265..329
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 475 AA; 51570 MW; A90CA00A569BF32A CRC64;
MMRFMALSTA LAVALGAATI NIQNMPPVQK RVGADSGNST IYSYHDSVKE ATKAVVNIST
QKKIKSNFMG GGMFNDPFFQ QFFGDLYNAI PKDRIERALG SGVVISKNGY IVTNNHVIDG
ADKISVTIPG SNKEYSATLV GTDADSDLAV IKINKENLPV IQFSDSSTTL VGDLVFAIGN
PFGVGETVTQ GIVSALNKTG IGINNYENFI QTDAAINPGN SGGALIDSRG GLVGINTAIL
SRTGGNHGVG FAIPSNTVKH IATQLIRTGT IHRGYLGVGI QDVSSELQDS YNGKEGAVVI
SIEKDSPAKK AGLMIWDLII EVNGKRVKNA AELRNLIGSL APNQHITIKY IRNKREYTTS
LVLAERKNPN RRETSTTHEG VNGQLSGIKV ETLTPRLRKE AHIPENIHGV FIQDVKDNSK
AQELGFRQGD VIMQIENVSI RNIEDFNRAL TRYRNITKRF LVFDPNRGYK QIVAK
//
