ID U5S336_9CLOT Unreviewed; 463 AA.
AC U5S336;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Dipeptidase PepV {ECO:0000313|EMBL:AGY78053.1};
DE EC=3.4.13.- {ECO:0000313|EMBL:AGY78053.1};
GN Name=pepV {ECO:0000313|EMBL:AGY78053.1};
GN ORFNames=CAETHG_3852 {ECO:0000313|EMBL:AGY78053.1};
OS Clostridium autoethanogenum DSM 10061.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY78053.1, ECO:0000313|Proteomes:UP000017590};
RN [1] {ECO:0000313|EMBL:AGY78053.1, ECO:0000313|Proteomes:UP000017590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY78053.1};
RX PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT "Comparison of single-molecule sequencing and hybrid approaches for
RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT systems in industrial relevant Clostridia.";
RL Biotechnol. Biofuels 7:40-40(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP006763; AGY78053.1; -; Genomic_DNA.
DR RefSeq; WP_023163436.1; NZ_CP012395.1.
DR AlphaFoldDB; U5S336; -.
DR KEGG; cah:CAETHG_3852; -.
DR PATRIC; fig|1341692.11.peg.3872; -.
DR HOGENOM; CLU_031786_2_0_9; -.
DR Proteomes; UP000017590; Chromosome.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd03888; M20_PepV; 1.
DR Gene3D; 3.30.70.360; -; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010964; M20A_pepV-rel.
DR InterPro; IPR002933; Peptidase_M20.
DR NCBIfam; TIGR01887; dipeptidaselike; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 4: Predicted;
KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997, ECO:0000313|EMBL:AGY78053.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGY78053.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022997, ECO:0000313|EMBL:AGY78053.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 463 AA; 51033 MW; 13F99EA90AC41E5C CRC64;
MELNKKVDEM KKELIKATQE VVRIKSTLDE EKPGMPFGEG PAKALEKALE IAAELGFHTY
KEEEGYYGYA EYGEGEDYVA VLGHMDVVPE GDNWIYPPYG AEIHEDKIFG RGTLDDKGAT
MAALFGLKAI KDLKMPLSKK VRVIFGTNEE TGSSEMHVYN KKEKAPVSGF TPDAMYPLIN
AEKGIRRFHV VKKLTSCNCG IAIKSLKGGI RPNMVPDKCE TVISIKNTED MVKAVKEFAD
KKGYNMKTEI VNGDVVLHTF GVGAHGSMPE LGKNAVMQTF DFLGTIAKGS CPLADYINFF
NKYVGFETEG TSLGIACEDK PSGKLSLNVG VAEINEETAD LWLDMRYPVT KKGEEIMDTL
SKKFAECGAK IERVEADEPL YFAEDSELVK TLLKVYNDET GQEGKAYGIG GGTYAKELPN
IIGFGPIFPG KPDLDHQANE YIEIGDLVMN AKIYAHAIYE LAK
//
