Y1176_CORGB
ID Y1176_CORGB Reviewed; 278 AA.
AC A4QD57;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Uncharacterized peptidase cgR_1176;
DE Flags: Precursor;
GN OrderedLocusNames=cgR_1176;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1] {ECO:0000312|EMBL:BAF54154.1}
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 33-52, 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 S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AP009044; BAF54154.1; -; Genomic_DNA.
DR RefSeq; WP_003858612.1; NC_009342.1.
DR AlphaFoldDB; A4QD57; -.
DR SMR; A4QD57; -.
DR EnsemblBacteria; BAF54154; BAF54154; cgR_1176.
DR GeneID; 58310215; -.
DR KEGG; cgt:cgR_1176; -.
DR HOGENOM; CLU_091277_0_0_11; -.
DR OMA; NQPEINC; -.
DR PhylomeDB; A4QD57; -.
DR Proteomes; UP000006698; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA: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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:19066885"
FT CHAIN 33..278
FT /note="Uncharacterized peptidase cgR_1176"
FT /evidence="ECO:0000269|PubMed:19066885"
FT /id="PRO_0000392966"
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; 28296 MW; 02509866DC90616E CRC64;
MSSASFTTKA LSVLAALTAA SAPLVAASPA HALANARNVT GSSTTSDSIV RLHIGNTACT
GTMITPTWAI TARHCIPEDG IAGAAIGSST LSQFQQVSQA ILHPTADLAL VELPNQASSN
TVDLYGAHVQ PGENGQAAGW GGYSAFGQNV AQQADVQIQR RVVNVPSPDR TAVLLEGTVS
NGRLVPGDSG GPLYINGQLA GVLSMSTDVE NDALDGTVGW YIPVAEHAEW IAYYTGKHIA
PIAGAPAELV DATANPTFIP APQPFTGSSI GGWALGSS