PEPT_BACAN
ID PEPT_BACAN Reviewed; 410 AA.
AC Q81WU4; Q6HUZ7; Q6KP72;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
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}; Synonyms=pepT-1;
GN OrderedLocusNames=BA_3872, GBAA_3872, BAS3588;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000255|HAMAP-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; AE016879; AAP27607.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT32987.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT55892.1; -; Genomic_DNA.
DR RefSeq; NP_846121.1; NC_003997.3.
DR RefSeq; WP_000656974.1; NZ_WXXJ01000001.1.
DR RefSeq; YP_029841.1; NC_005945.1.
DR PDB; 3IFE; X-ray; 1.55 A; A=1-410.
DR PDBsum; 3IFE; -.
DR AlphaFoldDB; Q81WU4; -.
DR SMR; Q81WU4; -.
DR IntAct; Q81WU4; 5.
DR STRING; 260799.BAS3588; -.
DR MEROPS; M20.003; -.
DR DNASU; 1088747; -.
DR EnsemblBacteria; AAP27607; AAP27607; BA_3872.
DR EnsemblBacteria; AAT32987; AAT32987; GBAA_3872.
DR GeneID; 45023569; -.
DR KEGG; ban:BA_3872; -.
DR KEGG; bar:GBAA_3872; -.
DR KEGG; bat:BAS3588; -.
DR PATRIC; fig|198094.11.peg.3842; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_053676_0_0_9; -.
DR OMA; GHNFHGK; -.
DR EvolutionaryTrace; Q81WU4; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-UniRule.
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 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 PANTHER; PTHR42994:SF1; PTHR42994:SF1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01882; peptidase-T; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..410
FT /note="Peptidase T"
FT /id="PRO_0000185277"
FT ACT_SITE 81
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT HELIX 1..13
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 30..46
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3IFE"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3IFE"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:3IFE"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3IFE"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 273..286
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 287..308
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:3IFE"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:3IFE"
FT HELIX 389..409
FT /evidence="ECO:0007829|PDB:3IFE"
SQ SEQUENCE 410 AA; 45911 MW; 6A57C9A46824FF7A CRC64;
MKEELIERFT RYVKIDTQSN EDSHTVPTTP GQIEFGKLLV EELKEVGLTE VTMDDNGYVM
ATLPANTDKD VPVIGFLAHL DTATDFTGKN VKPQIHENFD GNAITLNEEL NIVLTPEQFP
ELPSYKGHTI ITTDGTTLLG ADDKAGLTEI MVAMNYLIHN PQIKHGKIRV AFTPDEEIGR
GPAHFDVEAF GASFAYMMDG GPLGGLEYES FNAAGAKLTF NGTNTHPGTA KNKMRNATKL
AMEFNGHLPV EEAPEYTEGY EGFYHLLSLN GDVEQSKAYY IIRDFDRKNF EARKNTIENI
VKQMQEKYGQ DAVVLEMNDQ YYNMLEKIEP VREIVDIAYE AMKSLNIEPN IHPIRGGTDG
SQLSYMGLPT PNIFTGGENY HGKFEYVSVD VMEKAVQVII EIARRFEEQA