ID A0A081K6J2_9GAMM Unreviewed; 406 AA.
AC A0A081K6J2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Peptidase T {ECO:0000313|EMBL:KEI69768.1};
DE EC=3.4.11.4 {ECO:0000313|EMBL:KEI69768.1};
GN ORFNames=GV64_02545 {ECO:0000313|EMBL:KEI69768.1};
OS Endozoicomonas elysicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=305900 {ECO:0000313|EMBL:KEI69768.1, ECO:0000313|Proteomes:UP000027997};
RN [1] {ECO:0000313|EMBL:KEI69768.1, ECO:0000313|Proteomes:UP000027997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22380 {ECO:0000313|EMBL:KEI69768.1,
RC ECO:0000313|Proteomes:UP000027997};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KEI69768.1}.
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DR EMBL; JOJP01000001; KEI69768.1; -; Genomic_DNA.
DR RefSeq; WP_020582625.1; NZ_JOJP01000001.1.
DR AlphaFoldDB; A0A081K6J2; -.
DR STRING; 305900.GV64_02545; -.
DR eggNOG; COG2195; Bacteria.
DR Proteomes; UP000027997; Unassembled WGS sequence.
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 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 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 Aminopeptidase {ECO:0000313|EMBL:KEI69768.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KEI69768.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000027997}.
FT DOMAIN 209..310
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 406 AA; 44651 MW; 9EF29F0D44B5CFBC CRC64;
MNIEQVLVDY FHRYLAISSQ SDSQATIVPS SEGQRALAIQ LQNDLGAMGY DETKLLDNST
LIAHFPGNKP SAKKLGFVAH LDTVDVGLSP DIKPQQLHYS GSPLCLNKGQ NIIVSEESHP
ELARYLGQEI LFSDGTSVLG ADNKAAIAVM MTLAKSLWED PVDHGDLYFA FTPDEEIGLR
GAKELPMELF PVDHCYTIDC CERGEVIHET FNAGSAVLNI EGITAHPMSA KNVLVNPNLV
ATDFINMLND MGKPEQTDGR EGYFWVTDIQ GCQNKACVSV SIRDFDLTGY ESRKQYLESL
AKFLKTKHPK AVIQLSITDI YSNIAQAMGG DIEALDRLYQ VLSDLEIPAK SIAMRGGTDG
SALSAKGLFT PNFFTGAHNF HSPFEFLPIP SFVDSYRVAY RLMEIA
//
