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Database: UniProt
Entry: H0A7S5_9PROT
LinkDB: H0A7S5_9PROT
Original site: H0A7S5_9PROT 
ID   H0A7S5_9PROT            Unreviewed;       427 AA.
AC   H0A7S5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Peptidase T {ECO:0000313|EMBL:EHL96414.1};
GN   ORFNames=HMPREF9946_04882 {ECO:0000313|EMBL:EHL96414.1};
OS   Acetobacteraceae bacterium AT-5844.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae.
OX   NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHL96414.1, ECO:0000313|Proteomes:UP000003292};
RN   [1] {ECO:0000313|EMBL:EHL96414.1, ECO:0000313|Proteomes:UP000003292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHL96414.1}.
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DR   EMBL; AGEZ01000214; EHL96414.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0A7S5; -.
DR   STRING; 1054213.HMPREF9946_04882; -.
DR   PATRIC; fig|1054213.3.peg.4435; -.
DR   eggNOG; COG2195; Bacteria.
DR   HOGENOM; CLU_053676_0_0_5; -.
DR   OrthoDB; 9804934at2; -.
DR   BioCyc; ABAC1054213:G1H32-4502-MONOMER; -.
DR   Proteomes; UP000003292; Unassembled WGS sequence.
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   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; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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   Reference proteome {ECO:0000313|Proteomes:UP000003292};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT   DOMAIN          210..305
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        177
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         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         383
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ   SEQUENCE   427 AA;  46970 MW;  6A72657F9BB7AAAB CRC64;
     MVKPVEEQLV ERFFRYLAVA SQSDVRATSL PSTPGQLRLA RLLSEELEFL KASDIHLDEN
     GILTARIPGT VPDAPCIGFV AHLDTVDVGL SPAIRPQRLR FQGDDLLLNK EAGIWLRVDD
     HPEILPYKGE EILFGDGTSV LGADNKAAIA VVMTLVEEFL RKRPRHGDIV VAFVPDEEIG
     LRGAKALDLA RFPAAFAYTI DCCERGEVVY ETFNAASVEI NITGVPAHPM SAKGVLVNPI
     LVAADLMSLF DRKQTPEHTA GREGYWWFNG ITGDQSAAQI KMAIRDFDAE IFEERKSFVL
     ESVEKIQERF PRAKIECRIE DSYRNIAAAL GGKRDSVDLV LRAMAELGIT SKVVAMRGGT
     DGSALSARGL PTPNYFTGAL NFHSRFEFLP ISSFCDSFRV TQRICELAAE RGASVLRPNA
     RSDSSMG
//
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