ID   Y1093_CORGL             Reviewed;         278 AA.
AC   Q8NRF6; Q6M673;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Putative peptidase Cgl1093;
DE   Flags: Precursor;
GN   OrderedLocusNames=Cgl1093, cg1243;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2] {ECO:0000312|EMBL:CAF19799.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A4QD57}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; BA000036; BAB98486.1; -; Genomic_DNA.
DR   EMBL; BX927151; CAF19799.1; -; Genomic_DNA.
DR   RefSeq; NP_600321.1; NC_003450.3.
DR   RefSeq; WP_011014118.1; NC_006958.1.
DR   AlphaFoldDB; Q8NRF6; -.
DR   SMR; Q8NRF6; -.
DR   STRING; 196627.cg1243; -.
DR   KEGG; cgb:cg1243; -.
DR   KEGG; cgl:Cgl1093; -.
DR   PATRIC; fig|196627.13.peg.1072; -.
DR   eggNOG; COG5640; Bacteria.
DR   HOGENOM; CLU_091277_0_0_11; -.
DR   OMA; NQPEINC; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..278
FT                   /note="Putative peptidase Cgl1093"
FT                   /id="PRO_0000392965"
FT   DOMAIN          33..236
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000250|UniProtKB:P07288,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        74
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P07288,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        123
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P07288,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        189
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P07288,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        59..75
FT                   /evidence="ECO:0000250|UniProtKB:Q6H321,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   278 AA;  28238 MW;  130E389AEDCF62A0 CRC64;
     MSSASFTTKA LSVLAALTAA SAPLVAASPA HALANARNVT GSSTTSDSIV RLHIGNTACT
     GTMITPTWAI TARHCIPEGG IAGAAIGSST LSQFQQVSQA ILHPTADLAL VELPNQASSN
     TVDLYGAHVQ PGENGQAAGW GGYSAFGQNV AQQADVQIQR RVVNVPSPDR TAVLLEGTVS
     NGRLVPGDSG GPLYINGQLA GVLSMSTDVE NDALDGTVGW YIPVAEHAEW IAYYTGKHIA
     PIAGAPAELV DATANPTFIP APQPFTGSSI GGWALGSS