ID F5X497_STRPX Unreviewed; 355 AA.
AC F5X497;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Glutamyl aminopeptidase {ECO:0000313|EMBL:BAK29237.1};
DE EC=3.4.11.7 {ECO:0000313|EMBL:BAK29237.1};
GN Name=pepA {ECO:0000313|EMBL:BAK29237.1};
GN OrderedLocusNames=SGPB_0100 {ECO:0000313|EMBL:BAK29237.1};
OS Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK29237.1, ECO:0000313|Proteomes:UP000007946};
RN [1] {ECO:0000313|EMBL:BAK29237.1, ECO:0000313|Proteomes:UP000007946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC {ECO:0000313|Proteomes:UP000007946};
RX PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA Chang C.-H., Hsu M.-T.;
RT "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL PLoS ONE 6:E20519-E20519(2011).
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|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR EMBL; AP012054; BAK29237.1; -; Genomic_DNA.
DR RefSeq; WP_003062933.1; NC_015600.1.
DR AlphaFoldDB; F5X497; -.
DR STRING; 981540.SGPB_0100; -.
DR MEROPS; M42.001; -.
DR GeneID; 76469159; -.
DR KEGG; stb:SGPB_0100; -.
DR HOGENOM; CLU_047249_0_2_9; -.
DR Proteomes; UP000007946; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05656; M42_Frv; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017538; Pept_M42_glutamyl_aminopept.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR NCBIfam; TIGR03107; glu_aminopep; 1.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:BAK29237.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAK29237.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007946}.
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 355 AA; 38471 MW; 58878390E4F54D1B CRC64;
MSELFSKIKE ITELDSIAGY EHSVRNYLRS KITPLVDDVQ TDGLGGIFGI KNSAAENAPR
IMVAAHMDEV GFMVSDIKAD GTMRAVGIGG WNPLVLSSQR FTLYTRDGRA IPVVSGSVPP
HFLRGANGSA ALPKIDDIIF DAGFTDKAEA EAFGILPGDI IVPKSETILT ANQKNVISKA
WDNRFGVLMV TELLESLKGQ KLDNTLIAGA NVQEEVGLRG AHVSATKFQP ELFFAVDCSP
AGDIYGNQGK IGDGTLFRFY DPGHIMLKDM RDFLLTTAEE SGIKYQYYAA KGGTDAGAAH
LKNGGIPSTT IGVCARYIHS HQSLYAMDDF LQAQAFLQAI VKKLDRSTVD LIKKY
//
