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Database: UniProt
Entry: Q834H3_ENTFA
LinkDB: Q834H3_ENTFA
Original site: Q834H3_ENTFA 
ID   Q834H3_ENTFA            Unreviewed;       477 AA.
AC   Q834H3;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:AAO81457.1};
GN   OrderedLocusNames=EF_1679 {ECO:0000313|EMBL:AAO81457.1};
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO81457.1, ECO:0000313|Proteomes:UP000001415};
RN   [1] {ECO:0000313|EMBL:AAO81457.1, ECO:0000313|Proteomes:UP000001415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA   Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA   Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA   Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA   Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR   EMBL; AE016830; AAO81457.1; -; Genomic_DNA.
DR   RefSeq; NP_815387.1; NC_004668.1.
DR   AlphaFoldDB; Q834H3; -.
DR   STRING; 226185.EF_1679; -.
DR   MEROPS; S41.007; -.
DR   EnsemblBacteria; AAO81457; AAO81457; EF_1679.
DR   KEGG; efa:EF1679; -.
DR   PATRIC; fig|226185.45.peg.1831; -.
DR   eggNOG; COG0793; Bacteria.
DR   eggNOG; COG3409; Bacteria.
DR   HOGENOM; CLU_017295_3_0_9; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:AAO81457.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001415};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          97..166
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   477 AA;  51911 MW;  001A6DD2FE9FBF19 CRC64;
     MKNKRTVPFY QYIISLLCVA FLAGGSSYIY FDHRVKKMSQ EGAITNADLS KVQDLYNEIS
     TNYVGEVDKN ELVEGALKGM SEAIGDPYST YLNESAANDL NESLSGDFEG IGATMTMKDG
     EPVVAEAPVA DSPAEKAGIK EGDIIEKVDG TATKGMKLAE VVSKVRGKKG TSVELTIQRE
     GETKNISIKR GKIPVKTVTG ELDKNDAQIG SIKITSFGKK TYQELKETIT NLRDKGAKSF
     VIDVRQNPGG LLDQAERMAS MFLKNGETIV QFEDKKGRTM KEVASKELDG GFKVKEPVAV
     IIDGNSASAS EIFAAALHES ANVPLIGTKT FGKGTVQTVK DLNDQTEIKL TVLKWLTPKG
     EWINEKGIEP TIKADYPEYA YLKLIPRDKT LKEGDQSEDI QNLNAILAVL AYPVDENNAN
     YTAETKAAVS DLQQKNGLPV TGEIDNETAT KIEATLGKLI LENDAAYDTA VKEIQKN
//
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