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Database: UniProt
Entry: G9AEB8_RHIFH
LinkDB: G9AEB8_RHIFH
Original site: G9AEB8_RHIFH 
ID   G9AEB8_RHIFH            Unreviewed;       410 AA.
AC   G9AEB8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Peptidase T {ECO:0000313|EMBL:CCE99400.1};
DE            EC=3.4.11.4 {ECO:0000313|EMBL:CCE99400.1};
GN   Name=pepT {ECO:0000313|EMBL:CCE99400.1};
GN   OrderedLocusNames=SFHH103_04934 {ECO:0000313|EMBL:CCE99400.1};
OS   Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OG   Plasmid pSfHH103e {ECO:0000313|EMBL:CCE99400.1,
OG   ECO:0000313|Proteomes:UP000007735}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE99400.1, ECO:0000313|Proteomes:UP000007735};
RN   [1] {ECO:0000313|EMBL:CCE99400.1, ECO:0000313|Proteomes:UP000007735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH103 {ECO:0000313|EMBL:CCE99400.1,
RC   ECO:0000313|Proteomes:UP000007735};
RC   PLASMID=pSfHH103e {ECO:0000313|Proteomes:UP000007735};
RX   PubMed=22374952; DOI=10.1128/JB.06729-11;
RA   Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA   Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA   Vinardell J.M., Zehner S., Gottfert M.;
RT   "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL   J. Bacteriol. 194:1617-1618(2012).
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; HE616899; CCE99400.1; -; Genomic_DNA.
DR   RefSeq; WP_014331060.1; NC_016815.1.
DR   AlphaFoldDB; G9AEB8; -.
DR   KEGG; sfh:SFHH103_04934; -.
DR   PATRIC; fig|380.5.peg.4483; -.
DR   HOGENOM; CLU_053676_0_0_5; -.
DR   Proteomes; UP000007735; Plasmid pSfHH103e.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-EC.
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:CCE99400.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCE99400.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR037215-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Plasmid {ECO:0000313|EMBL:CCE99400.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT   DOMAIN          210..304
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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         199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         381
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;  44357 MW;  8ABDE0A99CB132C0 CRC64;
     MADTVTDRFL RYVVIDTQSD PRSAAQPSTE KQKTLGRLLV EELLAIGLSD AHLDKHGYVY
     ATIPSNVDKP VPVICLCSHM DTAPDFTGTN VKPQIVRNYA GGDIRLPGDP RQVIRVADNP
     ALADQIGNDI ITTDGTTLLG ADDKAGLAEI VTAAQVLVDN PDIPHGTIRL LFTTDEEIGR
     GVDKVDLQKL GADFAFTVDG ETAGHIEDET FSADSVDITI HGVAIHPGFA KDKMENAIKI
     AAAIVDGLPK DMAPETTAGR DGFVHPTGLS GSMEKATLSF IVRDFEEAGL ATKEAMLDEL
     ARRVIDDYPG SSYSFEVKQQ YRNMKAILDR HPEIVENAIE AIRRAGMTPV RGSIRGGTDG
     SRLSFMGLPS ANLFAGGHAF HSPLEWVSRQ DMERAVKTIV ELAKVWAERS
//
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