(data stored in SCRATCH zone)

SWISSPROT: A4AVH9_MARSH

ID   A4AVH9_MARSH            Unreviewed;       408 AA.
AC   A4AVH9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Peptidase T {ECO:0000256|HAMAP-Rule:MF_00550};
DE            EC=3.4.11.4 {ECO:0000256|HAMAP-Rule:MF_00550};
DE   AltName: Full=Aminotripeptidase {ECO:0000256|HAMAP-Rule:MF_00550};
DE            Short=Tripeptidase {ECO:0000256|HAMAP-Rule:MF_00550};
DE   AltName: Full=Tripeptide aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00550};
GN   Name=pepT {ECO:0000256|HAMAP-Rule:MF_00550};
GN   OrderedLocusNames=FB2170_01005 {ECO:0000313|EMBL:EAR00201.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00201.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00201.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides.
CC       {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|SAAS:SAAS00756406}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of the N-terminal residue from a tripeptide.;
CC         EC=3.4.11.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00550,
CC         ECO:0000256|SAAS:SAAS01122659};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-2};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-2};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00550,
CC       ECO:0000256|SAAS:SAAS00756389}.
CC   -!- SIMILARITY: Belongs to the peptidase M20B family.
CC       {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|SAAS:SAAS00756409}.
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DR   EMBL; CP002157; EAR00201.1; -; Genomic_DNA.
DR   RefSeq; WP_013304896.1; NC_014472.1.
DR   STRING; 313603.FB2170_01005; -.
DR   MEROPS; M20.003; -.
DR   EnsemblBacteria; EAR00201; EAR00201; FB2170_01005.
DR   KEGG; fbc:FB2170_01005; -.
DR   eggNOG; ENOG4105D42; Bacteria.
DR   eggNOG; COG2195; LUCA.
DR   HOGENOM; HOG000032390; -.
DR   KO; K01258; -.
DR   OMA; GHNFHGK; -.
DR   OrthoDB; 1015417at2; -.
DR   BioCyc; MSP313603:G1GNS-467-MONOMER; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03892; M20_peptT; 1.
DR   HAMAP; MF_00550; Aminopeptidase_M20; 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   PANTHER; PTHR42994:SF1; PTHR42994:SF1; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01882; peptidase-T; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AVH9.
DR   SWISS-2DPAGE; A4AVH9.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00550,
KW   ECO:0000256|SAAS:SAAS00756408};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00550,
KW   ECO:0000256|SAAS:SAAS00756401};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00550,
KW   ECO:0000256|SAAS:SAAS00786827};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00550,
KW   ECO:0000256|PIRSR:PIRSR037215-2, ECO:0000256|SAAS:SAAS00786925};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00550,
KW   ECO:0000256|SAAS:SAAS00756410};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00550,
KW   ECO:0000256|SAAS:SAAS00756386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-
KW   2, ECO:0000256|SAAS:SAAS00756404}.
FT   DOMAIN      207    305       M20_dimer. {ECO:0000259|Pfam:PF07687}.
FT   ACT_SITE     80     80       {ECO:0000256|HAMAP-Rule:MF_00550,
FT                                ECO:0000256|PIRSR:PIRSR037215-1}.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00550, ECO:0000256|PIRSR:PIRSR037215-
FT                                1}.
FT   METAL        78     78       Zinc 1. {ECO:0000256|HAMAP-Rule:MF_00550,
FT                                ECO:0000256|PIRSR:PIRSR037215-2}.
FT   METAL       141    141       Zinc 1. {ECO:0000256|HAMAP-Rule:MF_00550,
FT                                ECO:0000256|PIRSR:PIRSR037215-2}.
FT   METAL       141    141       Zinc 2. {ECO:0000256|HAMAP-Rule:MF_00550,
FT                                ECO:0000256|PIRSR:PIRSR037215-2}.
FT   METAL       176    176       Zinc 2. {ECO:0000256|HAMAP-Rule:MF_00550,
FT                                ECO:0000256|PIRSR:PIRSR037215-2}.
FT   METAL       198    198       Zinc 1. {ECO:0000256|HAMAP-Rule:MF_00550,
FT                                ECO:0000256|PIRSR:PIRSR037215-2}.
FT   METAL       379    379       Zinc 2. {ECO:0000256|HAMAP-Rule:MF_00550,
FT                                ECO:0000256|PIRSR:PIRSR037215-2}.
SQ   SEQUENCE   408 AA;  45912 MW;  417089EA75FCDD7E CRC64;
     MQQLIDRFLS YVKIDTQSDP NSETTPSTEK QWNLATELAY ELERIGLKDV IIDDNSYIMA
     TLPKNIEKEV PVIGFIAHFD TTPDFSGTNV NPQIIDDYDG KDIILNKEKN IILSPEYFDD
     LKQYEGQTLI TTDGTTLLGA DDKAGIAEII TAMEYLVEHP EIEHGDIKIG FTPDEEIGRG
     AQKFNTEKFG ADWAYTMDGS QIGELEYENF NAASAKVVIK GKSVHPGYAK GKMINAISIA
     TEFMGILPPE ETPQNTSGRE GFFHVHHMQG EIEHAEFELI IRDHDREHFE KRKNLLKKIA
     EKLNTTYGNC IQLEIKDQYF NMREKIEPVF HIVEIAKSAM EEVGISPIIK PIRGGTDGSQ
     LSYMGLPCPN IFAGGHNFHG KYEYVPVESM QKAVEVIVKI CELTASKI
//

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