ID A0A2X3W1T7_9STRE Unreviewed; 344 AA.
AC A0A2X3W1T7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=M42 glutamyl aminopeptidase {ECO:0000313|EMBL:SQF41209.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:SQF41209.1};
GN Name=ysdC {ECO:0000313|EMBL:SQF41209.1};
GN ORFNames=NCTC12278_01809 {ECO:0000313|EMBL:SQF41209.1};
OS Streptococcus ferus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1345 {ECO:0000313|EMBL:SQF41209.1, ECO:0000313|Proteomes:UP000249495};
RN [1] {ECO:0000313|EMBL:SQF41209.1, ECO:0000313|Proteomes:UP000249495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12278 {ECO:0000313|EMBL:SQF41209.1,
RC ECO:0000313|Proteomes:UP000249495};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; LS483343; SQF41209.1; -; Genomic_DNA.
DR RefSeq; WP_018030518.1; NZ_LS483343.1.
DR AlphaFoldDB; A0A2X3W1T7; -.
DR KEGG; sfer:NCTC12278_01809; -.
DR OrthoDB; 361940at2; -.
DR Proteomes; UP000249495; Chromosome 1.
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; cd05657; M42_glucanase_like; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF7; AMINOPEPTIDASE YHFE-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:SQF41209.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SQF41209.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000249495}.
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 344 AA; 38152 MW; 074BF3A90AA7E7E1 CRC64;
MSQTINYIQR LTNIPSPTGY TTEIMDYVAR EVTSYGYQAN RTNKGSIMVT VPGTNDQQHR
ILTAHLDTLG AIVRAVKPDG RLKMDLIGGF VYNAIEGENC TIHVSKNGHN ISGTILLHQT
SVHVYKDAGT AERNQDSMEI RLDEKVSTEA ETRALGIEVG DFISFDPRVV VTASGFIKSR
HLDDKVSAAI LLNLLKTYRE EKIQLPYTTH FYFSNNEEIG YGANSNIPEK VVEYLAVDMG
AMGDDQQTDE YSASICVKDG SGPYHYELRQ HLVSLAEKGN IPYKLDIYPY YGSDASAALR
AGSDVRHALL GAGIESSHSY ERTHIDSVQA TERLVDAYLK SKML
//
