ID E4Z7F6_DICNO Unreviewed; 474 AA.
AC E4Z7F6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Hydrolase AprB2 {ECO:0000313|EMBL:CBK25605.1};
DE Flags: Fragment;
GN Name=aprB2 {ECO:0000313|EMBL:CBK25605.1};
OS Dichelobacter nodosus (Bacteroides nodosus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=870 {ECO:0000313|EMBL:CBK25605.1};
RN [1] {ECO:0000313|EMBL:CBK25605.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21124876; DOI=10.1371/journal.ppat.1001210;
RA Kennan R.M., Wong W., Dhungyel O.P., Han X., Wong D., Parker D.,
RA Rosado C.J., Law R.H., McGowan S., Reeve S.B., Levina V., Powers G.A.,
RA Pike R.N., Bottomley S.P., Smith A.I., Marsh I., Whittington R.J.,
RA Whisstock J.C., Porter C.J., Rood J.I.;
RT "The subtilisin-like protease AprV2 is required for virulence and uses a
RT novel disulphide-tethered exosite to bind substrates.";
RL PLoS Pathog. 6:e1001210-e1001210(2010).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; FN674446; CBK25605.1; -; Genomic_DNA.
DR AlphaFoldDB; E4Z7F6; -.
DR SMR; E4Z7F6; -.
DR MEROPS; S08.040; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07496; Peptidases_S8_13; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034176; Peptidases_S8_13.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..474
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003194457"
FT DOMAIN 161..457
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 406
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 474
FT /evidence="ECO:0000313|EMBL:CBK25605.1"
SQ SEQUENCE 474 AA; 50219 MW; 68397A40A0332183 CRC64;
MKRFIMNKMA LVVCAALVGQ VASAETMVNY ASAKAIGKQP AGSVRFIVKY KDNSQSSKDL
KNRSTTKVMA NGMQVAGFNA QFVRMTGAGA GIFSVPDLKT TKEAHLVMDT IASNPDVEFV
EVDRIARPTA APNDQHYREQ WHYFDRYGVK ADKVWDMGFT GQNVVVAVVD TGILHHRDLN
ANVLPGYDFI SNSQISLDGD GRDADPFDEG DWFDNWACGG RPDPRKERSD SSWHGSHVAG
TIAAVTNNRI GVAGVAYGAK VVPVRALGRC GGYDSDISDG LYWAAGGRIA GIPENRNPAK
VINMSLGSDG QCSYNAQTMI DRATRLGALV VVAAGNENQN ASNTWPTSCN NVLSVGATTS
RGIRASFSNY GVDVDLAAPG QDILSTVDSG TRRPVSDAYS FMAGTSMATP HVSGVAALVI
SAANSVNKNL TPAELKDVLV STTSPFNGRL DRALGSGIVD AEAAVNSVLG NEGN
//
