ID PEPT_HAEIN Reviewed; 412 AA. AC P45172; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 141. DE RecName: Full=Peptidase T {ECO:0000255|HAMAP-Rule:MF_00550}; DE EC=3.4.11.4 {ECO:0000255|HAMAP-Rule:MF_00550}; DE AltName: Full=Aminotripeptidase {ECO:0000255|HAMAP-Rule:MF_00550}; DE Short=Tripeptidase {ECO:0000255|HAMAP-Rule:MF_00550}; DE AltName: Full=Tripeptide aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00550}; GN Name=pepT {ECO:0000255|HAMAP-Rule:MF_00550}; GN OrderedLocusNames=HI_1348; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides. CC {ECO:0000255|HAMAP-Rule:MF_00550}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of the N-terminal residue from a tripeptide.; CC EC=3.4.11.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00550}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00550}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00550}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}. CC -!- SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000255|HAMAP- CC Rule:MF_00550}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC22995.1; -; Genomic_DNA. DR PIR; C64118; C64118. DR RefSeq; NP_439499.1; NC_000907.1. DR AlphaFoldDB; P45172; -. DR SMR; P45172; -. DR STRING; 71421.HI_1348; -. DR MEROPS; M20.003; -. DR EnsemblBacteria; AAC22995; AAC22995; HI_1348. DR KEGG; hin:HI_1348; -. DR PATRIC; fig|71421.8.peg.1401; -. DR eggNOG; COG2195; Bacteria. DR HOGENOM; CLU_053676_0_0_6; -. DR OrthoDB; 9804934at2; -. DR PhylomeDB; P45172; -. DR BioCyc; HINF71421:G1GJ1-1373-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule. DR CDD; cd03892; M20_peptT; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR HAMAP; MF_00550; Aminopeptidase_M20; 1. DR InterPro; IPR001261; ArgE/DapE_CS. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR InterPro; IPR010161; Peptidase_M20B. DR NCBIfam; TIGR01882; peptidase-T; 1. DR PANTHER; PTHR42994; PEPTIDASE T; 1. DR PANTHER; PTHR42994:SF1; PEPTIDASE T; 1. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF037215; Peptidase_M20B; 1. DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1. DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1. PE 3: Inferred from homology; KW Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Zinc. FT CHAIN 1..412 FT /note="Peptidase T" FT /id="PRO_0000185298" FT ACT_SITE 86 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT ACT_SITE 179 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 146 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 146 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 180 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 202 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 385 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" SQ SEQUENCE 412 AA; 45986 MW; 7922E34B2B904A49 CRC64; MISQIDKTEL LERFLHYVSF HTQSKPNAKH SPSSVGQMKL AMQLQKELIQ LGLENVEVSK YAVVTAFLPA NDPNLTKTIG LVAHLDTSPQ CSGKNVRPEV IEEYRGGDIA LGIGEEFISP VYYSFMQKLV GQTLIVTDGT TLLGADNKAG IAEIMTALSI LQKENIPHCN IRVAFTPDEE IGLGIHYFPM EKFSCDWAYT IDGGEVGELE YENFNAATAK VRFFGRNIHT GYAKGKMLNA LTLACEFQQV FPVDEVPEKT DGKVGFYHLE DFSGDIEQVE LTYLIRDFDE QNFAQRKAFI KNQVEKFNAK KGLKKPIELE IQDSYQNMYD VVKNVPQSIE LADRAMKAVG IKPNHKPIRG GTDGAFLASK GLACPNIFTG GYNFHSKHEL VSLQGMENTV QVIIEMLKCK DL //