ID   Y2070_CORGB             Reviewed;         211 AA.
AC   A4QFQ3;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Probable endopeptidase cgR_2070;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=cgR_2070;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1] {ECO:0000312|EMBL:BAF55069.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 36-54, AND SUBCELLULAR LOCATION.
RX   PubMed=19066885; DOI=10.1007/s00253-008-1786-6;
RA   Suzuki N., Watanabe K., Okibe N., Tsuchida Y., Inui M., Yukawa H.;
RT   "Identification of new secreted proteins and secretion of heterologous
RT   amylase by C. glutamicum.";
RL   Appl. Microbiol. Biotechnol. 82:491-500(2009).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19066885}.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284, ECO:0000305}.
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DR   EMBL; AP009044; BAF55069.1; -; Genomic_DNA.
DR   RefSeq; WP_003856600.1; NC_009342.1.
DR   AlphaFoldDB; A4QFQ3; -.
DR   SMR; A4QFQ3; -.
DR   EnsemblBacteria; BAF55069; BAF55069; cgR_2070.
DR   GeneID; 58308866; -.
DR   KEGG; cgt:cgR_2070; -.
DR   HOGENOM; CLU_016043_6_0_11; -.
DR   OMA; VYYSGAS; -.
DR   PhylomeDB; A4QFQ3; -.
DR   Proteomes; UP000006698; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   Pfam; PF00877; NLPC_P60; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS51935; NLPC_P60; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Secreted; Signal;
KW   Thiol protease.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000269|PubMed:19066885"
FT   CHAIN           36..211
FT                   /note="Probable endopeptidase cgR_2070"
FT                   /id="PRO_0000392963"
FT   DOMAIN          97..211
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        127
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ   SEQUENCE   211 AA;  21245 MW;  FE5A5ACECB024D6C CRC64;
     MGKHRRNNSN ATRKAVAASA VALGATAAIA SPAQAAEVVV PGTGISVDIA GIETTPGLNN
     VPGIDQWIPS LSSQAAPTAY AAVIDAPAAE AQAAPAASTG QAIVDAARTK IGSPYGWGAT
     GPNAFDCSGL TSWAYSQVGK SIPRTSQAQA AQGTPVAYSD LQAGDIVAFY SGATHVGIYS
     GHGTVIHALN SSTPLSEHSL DYMPFHSAVR F