ID Q1JLX4_STRPC Unreviewed; 486 AA.
AC Q1JLX4;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Xaa-His dipeptidase {ECO:0000313|EMBL:ABF32095.1};
GN OrderedLocusNames=MGAS9429_Spy0907 {ECO:0000313|EMBL:ABF32095.1};
OS Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370551 {ECO:0000313|EMBL:ABF32095.1, ECO:0000313|Proteomes:UP000002433};
RN [1] {ECO:0000313|EMBL:ABF32095.1, ECO:0000313|Proteomes:UP000002433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS9429 {ECO:0000313|EMBL:ABF32095.1,
RC ECO:0000313|Proteomes:UP000002433};
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP000259; ABF32095.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1JLX4; -.
DR KEGG; spk:MGAS9429_Spy0907; -.
DR HOGENOM; CLU_031786_2_0_9; -.
DR Proteomes; UP000002433; Chromosome.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd03888; M20_PepV; 1.
DR Gene3D; 3.30.70.360; -; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010964; M20A_pepV-rel.
DR InterPro; IPR011291; Pept_M20A_peptidaseV.
DR InterPro; IPR002933; Peptidase_M20.
DR NCBIfam; TIGR01886; dipeptidase; 1.
DR NCBIfam; TIGR01887; dipeptidaselike; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 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 4: Predicted;
KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022997};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 486 AA; 53338 MW; 7DE223F23D848B98 CRC64;
MAYFKLNIIP KTNKESIMTT IDFKAEVDKR KEAMLADLVD LLRINSERDD TLADDKHPFG
PGPVKALEHF LAMAERDGYK TRNIDNYAGD FEFGQGDEVL GIFGHLDVVP AGSGWDTDPY
EPVIKDDRIY ARGSSDDKGP TMACYYALKI IKELGLPVSK KVRFIVGTDE ESGWGDMDYY
FAHNGLKNPD FGFSPDAEFP IINGEKGNIT EYLHFAGDNN GAFVLHRFQG GLRENMVPES
ATAVITSPHD LDVLEAALEQ FLSEHGVKGS MKATDGKIEV TIIGKSAHGS TPEAGVNGAT
LLAKFLNQFT FEGAAKDYLY VAGEVLHEDF AAEKLGLAYT DDRMGALSMN AGVFTFDSQS
ADNTIALNFR YPKGTDAATL KAGLEKLPGV IKVSLSEHEH TPHYVPMDDE LVATLLAVYE
KQTGLKGYEQ VIGGGTFGRL LERGVAFGAM FPGDENTMHQ ANEYMPLENI YRSAAIYAEA
IYELIK
//
