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Database: UniProt
Entry: Q8FP57_COREF
LinkDB: Q8FP57_COREF
Original site: Q8FP57_COREF 
ID   Q8FP57_COREF            Unreviewed;       467 AA.
AC   Q8FP57; C8NPN9;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=Putative periplasmic serine protease {ECO:0000313|EMBL:BAC18741.1};
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18741.1, ECO:0000313|Proteomes:UP000001409};
RN   [1] {ECO:0000313|EMBL:BAC18741.1, ECO:0000313|Proteomes:UP000001409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395
RC   {ECO:0000313|Proteomes:UP000001409};
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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DR   EMBL; BA000035; BAC18741.1; -; Genomic_DNA.
DR   RefSeq; WP_006767930.1; NZ_GG700683.1.
DR   AlphaFoldDB; Q8FP57; -.
DR   STRING; 196164.gene:10742359; -.
DR   KEGG; cef:CE1931; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_494218_0_0_11; -.
DR   OrthoDB; 73775at2; -.
DR   Proteomes; UP000001409; Chromosome.
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; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:BAC18741.1};
KW   Protease {ECO:0000313|EMBL:BAC18741.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001409}.
FT   DOMAIN          201..254
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   467 AA;  50082 MW;  D0C82050EA51766B CRC64;
     MTFDTLADAT VKIVGQGTFI EPGTVDPSES AWEGSGFIID PSGIAITNNH VVVGAGRLDG
     TYGENGESKA SMRVLGASEC LDLAVVQLNA DDLPHYTWYD GQITTGLDVY SAGFPAGASD
     DFTLTRGIVS KTDFEFDTQW ASLEHVIEHD ARIRGGNSGG PLITGDAKVL GVNYAGDDSL
     DYNFAIHRDV VRNVIDDMID GKRISSIGVN AQAWDSGDPE FFGVWVSSVE PGGPADKAGI
     EPGDLILKLG GVSVGDEGNL ASYCQVLDTH GSDGTMDVEV LRPRDDTLLT GQINGRELEV
     EQENVSGGQA TEQAGEYSGE SVEITDDSNS LAVSVPVEWA DVDPTPWKDN NGRDWVSLVA
     APDLDAFWAS YNAPGLWMLG TDPSYTPEQV LEQFDASGTC TETERDTWDD GYYRGPYVAY
     DCSGTTVLLL ATQDYDQTGP LALLIQLQTD YEVSTVLTEI ASTFRFI
//
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