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Database: UniProt
Entry: C5D435_GEOSW
LinkDB: C5D435_GEOSW
Original site: C5D435_GEOSW 
ID   C5D435_GEOSW            Unreviewed;       372 AA.
AC   C5D435;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Peptidase T-like protein {ECO:0000313|EMBL:ACS24991.1};
GN   OrderedLocusNames=GWCH70_2283 {ECO:0000313|EMBL:ACS24991.1};
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS24991.1};
RN   [1] {ECO:0000313|EMBL:ACS24991.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70 {ECO:0000313|EMBL:ACS24991.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000256|PIRSR:PIRSR001123-2};
CC   -!- SIMILARITY: Belongs to the peptidase M42 family.
CC       {ECO:0000256|PIRNR:PIRNR001123}.
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DR   EMBL; CP001638; ACS24991.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5D435; -.
DR   STRING; 471223.GWCH70_2283; -.
DR   MEROPS; M20.018; -.
DR   KEGG; gwc:GWCH70_2283; -.
DR   eggNOG; COG2195; Bacteria.
DR   HOGENOM; CLU_021802_6_0_9; -.
DR   OrthoDB; 9776600at2; -.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05683; M20_peptT_like; 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; IPR010162; PepT-like.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR008007; Peptidase_M42.
DR   NCBIfam; TIGR01883; PepT-like; 1.
DR   PANTHER; PTHR42994; PEPTIDASE T; 1.
DR   PANTHER; PTHR42994:SF2; T, PUTATIVE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001123; PepA_GA; 3.
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:PIRSR001123-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          180..274
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ   SEQUENCE   372 AA;  39463 MW;  7BFB421B9471A738 CRC64;
     MINQQRLVDE FLELVQIDSE TKHEGEIAKV LKQKFEALGL HVIEDDAAAK TGHGAGNLIC
     TLEATKEGVD PIYFTSHMDT VVPGKGVKPS IQDGYVVTDG TTILGADDKA GLAAMFEAIR
     VLKEQNIPHG TIQFIITVGE ESGLVGAKAL DPSLIQAKFG YALDSDGKVG NIVVAAPTQA
     KLKVVVHGKT AHAGVAPEKG VSAITIAAKA IAQMPLGRID EETTANIGRF EGGTQTNIVC
     DRVDILAEAR SLVPEKMEAQ VAKMKEAFET VAEEMGGRAE VDVEVMYPGF KFGDGDHVVE
     VAKRAAAKIG RPCELLRSGG GSDANVIAGF GIPTVNLAVG YEDIHTTNER MPIEELVKLT
     EMVVAIVEEV AK
//
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