Y2188_CORGL
ID Y2188_CORGL Reviewed; 209 AA.
AC Q8NNK6; Q6M3P5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable endopeptidase Cgl2188;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN OrderedLocusNames=Cgl2188, cg2402;
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:CAF20529.1}
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:A4QFQ3}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
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DR EMBL; BA000036; BAB99581.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20529.1; -; Genomic_DNA.
DR RefSeq; NP_601392.1; NC_003450.3.
DR RefSeq; WP_011014945.1; NC_006958.1.
DR AlphaFoldDB; Q8NNK6; -.
DR SMR; Q8NNK6; -.
DR STRING; 196627.cg2402; -.
DR KEGG; cgb:cg2402; -.
DR KEGG; cgl:Cgl2188; -.
DR PATRIC; fig|196627.13.peg.2125; -.
DR eggNOG; COG0791; Bacteria.
DR HOGENOM; CLU_016043_6_0_11; -.
DR OMA; VYYSGAS; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005576; C:extracellular region; ISS: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 3: Inferred from homology;
KW Hydrolase; Protease; Reference proteome; Secreted; Signal; Thiol protease.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..209
FT /note="Probable endopeptidase Cgl2188"
FT /id="PRO_0000392964"
FT DOMAIN 95..209
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 125
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ SEQUENCE 209 AA; 21044 MW; 9FB68AD8CC21BB50 CRC64;
MGKHRRNNSN ATRKAVAASA VALGATAAIA SPAQAAEVVV PGTGISVDIA GIETTPGLNN
VPGIDQWIPS LSSQAAPTAY AAVIDAPAAQ AAPAASTGQA IVDAARTKIG SPYGWGATGP
NAFDCSGLTS WAYSQVGKSI PRTSQAQAAQ GTPVAYSDLQ AGDIVAFYSG ATHVGIYSGH
GTVIHALNSS TPLSEHSLDY MPFHSAVRF
