ID Q666F9_YERPS Unreviewed; 410 AA.
AC Q666F9;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE SubName: Full=Probable peptidase PepT familly {ECO:0000313|EMBL:CAH22537.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:CAH22537.1};
GN OrderedLocusNames=YPTB3299 {ECO:0000313|EMBL:CAH22537.1};
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH22537.1, ECO:0000313|Proteomes:UP000001011};
RN [1] {ECO:0000313|EMBL:CAH22537.1, ECO:0000313|Proteomes:UP000001011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011};
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR037215-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR037215-
CC 2};
CC -!- SIMILARITY: Belongs to the peptidase M20B family.
CC {ECO:0000256|ARBA:ARBA00009692}.
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DR EMBL; BX936398; CAH22537.1; -; Genomic_DNA.
DR RefSeq; WP_011193029.1; NZ_CP009712.1.
DR AlphaFoldDB; Q666F9; -.
DR GeneID; 66844276; -.
DR KEGG; ypo:BZ17_3310; -.
DR KEGG; yps:YPTB3299; -.
DR PATRIC; fig|273123.14.peg.3472; -.
DR Proteomes; UP000001011; Chromosome.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03892; M20_peptT; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 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; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:CAH22537.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAH22537.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037215-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 209..311
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 84
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ SEQUENCE 410 AA; 44919 MW; E71AAD13399E6045 CRC64;
MTIALSEQLT NRFFRYLAVS SQSDAASPTL PSTEGQHKMA QMLAEELRQL GLEDILIDEH
ATVTARKPGN QPTAPRIGFI THIDTVDVGL SPDIHPQRLR FTGSDLCLNA EQGIYLRTAE
HPEILRYQGE EIIFSDGTSV LGADNKAAVT VVMTLLENLT ADDCHGDIVV AFVPDEEIGL
RGAKALDLAR FDVDFAYTID CCELGEVVYE NFNAASAEID IIGVTAHPMS AKNVLINPIR
VAYDIISEFS PQETPEHTEG REGYVWFTDM TANPNSAKLK IAIRDFDNVS FAARKAYIGE
VVAKVSAQYP RAKISYSVTD VYSNISNSIG EDKRAIDLIF SSMAELNIEP KVIPMRGGTD
GAALSTQGLL TPNYFTGAHN FHSPFEFLPI SSFVKSYQLT RTICLSAAKV
//
