ID D8EZX5_9DELT Unreviewed; 592 AA.
AC D8EZX5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Peptidase families S8 and S53 {ECO:0000313|EMBL:EFK10919.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:EFK10919.1};
GN ORFNames=NPH_5394 {ECO:0000313|EMBL:EFK10919.1};
OS delta proteobacterium NaphS2.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK10919.1, ECO:0000313|Proteomes:UP000003834};
RN [1] {ECO:0000313|EMBL:EFK10919.1, ECO:0000313|Proteomes:UP000003834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NaphS2 {ECO:0000313|EMBL:EFK10919.1,
RC ECO:0000313|Proteomes:UP000003834};
RX PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA Lipton M.S., Deboy R., Methe B.A.;
RT "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL PLoS ONE 5:E14072-E14072(2010).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:EFK10919.1}.
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DR EMBL; ADZZ01000154; EFK10919.1; -; Genomic_DNA.
DR AlphaFoldDB; D8EZX5; -.
DR Proteomes; UP000003834; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
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; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003834};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..592
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003114063"
FT DOMAIN 171..474
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 436
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 592 AA; 61534 MW; F2DD590633AD5574 CRC64;
MKGFILGIFI FCSLGVSAQG AATMVTAPEG VSPDLMNGLL NSPKIKRADM VLKDFLEERA
STTRVIVNLR ETETINTQKR MEKPHNREYV ANRIHDLVDG ILQGFSPAQL QNTRAFNYIA
GFSARVTPEG LASLAEDPDV LSIEKDALLY PNLAQGIPLM SASAVRSMYS GEGLSVAICD
TGIDYSHVAL GNGGFPNNKV IGGYDTGDDD NDPMDVEGHG TACAGIAAGN LGSDGDYIGG
VAWGAKLYAL KISHGRGGSA YLSNMIEAWE WCITHQYDDP DNPILIINTS FGVASFGSGR
FTGYCDSDSP AMTTAAANAK AAGITLFVSS GNDGYCDALE WPGCISHVVS VGAVYDAHFT
VNSIGWCVAQ DSCATKTPTG GCTSGYSSPE IPYEDQVPVY SNTATFLSLL APANWATTTK
LGGGYWTAAY GFGGTSAASP YAAGAAACLQ SAAKAITGSF LTPDQLQSIL VDTGDSITDV
KVAITKPRVN LGNAVAALGG GGSAIYVEPS GSCGGNSPCY TNIQDAVDAA ASGDIIEISQ
DTTAQAVSLN TAKNVTLQGG WNPSFTVQTS QTTVTSLNIQ KGSMSVDSLI LR
//
