ID   Q0AW74_SYNWW            Unreviewed;       497 AA.
AC   Q0AW74;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=C-terminal processing peptidase {ECO:0000313|EMBL:ABI69030.1};
DE            EC=3.4.21.102 {ECO:0000313|EMBL:ABI69030.1};
GN   OrderedLocusNames=Swol_1732 {ECO:0000313|EMBL:ABI69030.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI69030.1, ECO:0000313|Proteomes:UP000001968};
RN   [1] {ECO:0000313|Proteomes:UP000001968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR   EMBL; CP000448; ABI69030.1; -; Genomic_DNA.
DR   RefSeq; WP_011641127.1; NC_008346.1.
DR   AlphaFoldDB; Q0AW74; -.
DR   STRING; 335541.Swol_1732; -.
DR   KEGG; swo:Swol_1732; -.
DR   eggNOG; COG0793; Bacteria.
DR   eggNOG; COG3409; Bacteria.
DR   HOGENOM; CLU_017295_3_0_9; -.
DR   Proteomes; UP000001968; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00988; PDZ_CTP_protease; 1.
DR   CDD; cd07560; Peptidase_S41_CPP; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.30.750.44; -; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004447; Peptidase_S41A.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR005151; Tail-specific_protease.
DR   NCBIfam; TIGR00225; prc; 1.
DR   PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF03572; Peptidase_S41; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00245; TSPc; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:ABI69030.1};
KW   Protease {ECO:0000256|RuleBase:RU004404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001968};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..497
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038439934"
FT   DOMAIN          84..151
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   497 AA;  54690 MW;  0BAADFE48C52F5A7 CRC64;
     MKNQNLVVLI ILSLVMLLLA PLGSAIPANA ADAADNSYLQ EMMHFIKDRY YFEVNEEQIT
     QGALKGMFQG LDDYSDFFTR EEAQVMLESV EGNYEGIGVA LSKVDNYIVI TRVFPSSPAE
     SAGLLSGDRL VTVDKKDVLG YSVEQVSTLI RGPKDSLVNL GIVRNGIKNV VEFRVKREDI
     KLNPVRYENR GGIGYIAIDS FNSNTAEFLV TVLEAAEKDG ISKLVLDLRD NTGGEVTQAV
     AVARHFVPAG PITTIKFKAA GMKDKVYTSE LSAPPYKLVV LVNGMTASAS EIVAGAIQDS
     QAGVLLGSKT YGKARVQAII PLLSPEAYQK YARLYPDTSL DSNEMLIHHG IQATDREIMG
     WAKITTGIYI TPSGKYIDGQ GLLPDIKVSD PTPLNGWEIS NLMPLEKSGK PALNSSSLEV
     YNAEKILSAS GYELDKPDMT LDIKTFNAIK KFQQEQRLYP SGILDFTTQE ALNRKRQELI
     NCYDQQYARA VEYLLGR
//